AU2011218624B2 - Agents and methods for diagnosing stress - Google Patents

Abstract

This invention relates generally to methods and agents for determining the status of the immune system. More particularly, the present invention relates to molecules and assays for qualitatively or quantitatively determining the effect of stress on the immune system, the susceptibility to developing disease or illness through immune system dysfunction as a result of stress, and for monitoring the ability of an animal to cope with stress. The invention is useful inter alia in measuring response to immunomodulatory therapies, and monitoring the immune response to natural disease under stressful conditions. In certain embodiments, the invention is useful for monitoring animals in athletic training, for measuring the effects of aging on ability to respond to stress and external stressors, and for enabling better treatment and management decisions to be made in animals at risk of exposure to disease, or susceptible to disease through the effects of stress.

Description

Australian Patents Act 1990 - Regulation 3.2 ORIGINAL COMPLETE SPECIFICATION STANDARD PATENT Invention Title: "Agents and methods for diagnosing stress" The following statement is a full description of this invention, including the best method of performing it known to us: P/00/01I C\NRPortbl\DCC\RR\3841143_ .DOC - 29/8/11 TITLE OF THE INVENTION "AGENTS AND METHODS FOR DIAGNOSING STRESS This application is a divisional of Australian Patent Application No. 2005250056, the entire content of which is incorporated herein by reference. 5 FIELD OF THE INVENTION [0001] This invention relates generally to methods and agents for determining the status of the immune system. More particularly, the present invention relates to molecules and assays for qualitatively or quantitatively determining the effect of stress on the immune system, the susceptibility to developing disease or illness through immune system dysfunction as a 10 result of stress, and for monitoring the ability of an animal to cope with stress. The invention is useful inter alia in measuring response to immunomodulatory therapies, and monitoring the immune response to natural disease under stressful conditions. In certain embodiments, the invention is useful for monitoring animals in athletic training, for measuring the effects of aging on ability to respond to stress and external stressors, and for enabling better treatment and 15 management decisions to be made in animals at risk of exposure to disease, or susceptible to disease through the effects of stress. BACKGROUND OF THE INVENTION [00021 The immune system functions to protect an organism from foreign invasion and insults. The host immune system of mammals can be functionally divided into adaptive and 20 innate components. Innate immunity is often the first line of defense to external insults and consists of natural barriers, such as keratinous surfaces, secretions and chemicals, for example skin, mucous, lysozyme and acute phase proteins. The innate immune system can be found in most organisms, is non-specific, and many defense molecules that are part of the innate immune system are evolutionally conserved across a broad range of species (e.g., complement 25 components appear early in evolution in invertebrates). [00031 The adaptive immune system produces a specific response and "remembers" an infectious or invading agent to enable the host to engender an anamnestic response upon a subsequent challenge. The adaptive immune system can also be functionally divided into humoral and cellular components. The humoral component consists of soluble factors, and in 30 mammals this consists of antibodies. Cells of the immune system of higher organisms consist of the lymphoid or mycloid lines. Lymphoid cells differentiate in the thymus (T cells) or bone marrow (B cells). B cells and T cells are morphologically identical. Myeloid cells are phagocytes and other cells such as platelets and mast cells. Phagocytes are either monocytes or polymorphonuclear cells. [For a general review of the immune system and its cellular and 35 humoral components, see "Essential Immunology," 10a edition, Roitt and Delves, Blackwell Publishing 2001; and "Immunobiology. The Immune system in Health and Disease," 4 d' edition, Janeway et al., Garland Publishing 1999]. -1 - [00041 Functional studies of the immune system of mammals constitute a vast body of literature and there are numerous tests available to measure the functional capabilities of the immune system. The humoral immune system is more amenable to functional testing as compared to the cellular immune system. For example, antibodies bind specifically to their 5 target molecules and can be measured directly in tests such as antibody diffusion and precipitation assays, enzyme-linked immunosorbent assays, or used to detect the presence of invading organisms in antigen capture assays. [00051 The function of the cellular immune system is more difficult to measure and often involves simple counting of the numbers of various subpopulations of cells using stains or 10 specific antibodies to cell surface proteins. For example, one of the most common blood tests in medicine is a complete blood count (CBC) that measures red and white blood cell and platelet numbers. A differential white cell count uses Wright stain to enable the enumeration of lymphocytes, neutrophils, basophils, eosinophils and monocytes. Infection with bacteria often results in increased numbers of neutrophils in peripheral blood samples, and parasitic infections 15 often results in increased numbers of eosinophils. However, counting the numbers of white blood cell types in a peripheral blood sample is often a poor indicator of the functional capabilities of the immune system, it is non-specific (not capable of determining the nature of infection or insult) and lymphocytes of the B and T cell lineage cannot be distinguished. [00061 B lymphocytes produce antibodies and T lymphocytes are one of the main 20 regulators and effectors of the immune system. Various subpopulations of B and T cells can be distinguished on the basis of different proteins (markers) on their cell surface. B cells express immunoglobulin (antibody) proteins on their cell surface and T cells express various markers depending upon their stage of development and function. Many different reagents (often antibodies) have been developed to differentiate subpopulations of T and B cells in humans and 25 experimental animal species and many can be bought commercially from companies such as Alexis Corporation (www.alexis-corp.com). Again, simply counting the numbers of B and T cells (including subpopulations) is not informative on the functional capabilities of the cells. The preparation of reagents for detecting cell surface markers is also laborious and a highly specialized activity. 30 [00071 There are more direct methods of measuring immune cell function, including; plaque forming, chemotaxis, random migration, superoxide anion release, concentration of ATP in circulating CD4* cells following in vitro stimulation with phytohemagglutinin, and release of fluorescent dye from target cells assays. Many of these tests are laborious, require prior cell preparation and purification methods (often affecting the results 35 of subsequent assays), and only measure the function of one particular subset of cells. -2- [0008] In summary, there currently exists a need for more effective modalities for measuring the functional capabilities of the immune system, and particularly the cellular immune system. [0009] Athletic performance animals are unable to communicate their well-being to 5 human owners or trainers. In addition, human athletes are often unaware of their well-being (due to heavy training) or are unable to communicate this effectively to trainers or medical practitioners. Therefore, there is also a need for more effective methods for monitoring the functional capabilities of the cellular immune system, especially in athletic performance animals. 10 [00101 It is almost 70 years since it was first recognized that stress can activate a physiological response that may be beneficial or damaging to the body (Seyle H. 1936, Nature 138:32), Stress is a physical, chemical or emotional factor that causes bodily or mental tension and may be a factor in disease causation. A publication by Pedersen et al. (1994, Inter J. Sports Med. 15:5116-5121) provides a review of work conducted in the area of stress and disease. 15 [0011] In recent years, rapid advances in the field of immunology have generated intense interest in the interaction between stress induced by psychosocial, nutritional and physical factors and the immune system. A major premise of this work is that stress may enhance vulnerability to disease by exerting an immunosuppressive effect. This may especially be true of diseases intimately connected with immunologic mechanisms such as infection, 20 malignancy and autoimmune disease. [0012] Studies demonstrating immune alterations in stress encompass a number of models in which most types of experimental and naturally occurring stresses have been associated with alteration of the components of the immune system. Some of the earliest work was conducted by the United States National Aeronautic Space Administration (NASA). The 25 NASA studies showed that white blood cells and T-lymphocytes were elevated during the splash-down phase of space flight. However, there was impairment in the lymphoproliferative response to mitogenic stimulation during the first three (3) days after return to earth. A slight decrease in the stimulation response of lymphocytes was also observed prior to launch, possibly due to anticipation. A general overview of stress and immune function can be found in "Stress, 30 Immunity and Illness--A Review", authored by Dorian and Garfinkel, Psychological Medicine, 17:393-407 (1987). [00131 Physical activity and exercise are also known to produce a variety of alterations to the immune system. The effects of vigorous exercise appear to depress immune function and may compromise host defenses against upper respiratory tract infections. 35 Epidemiological studies have generally shown a greater risk of upper respiratory tract infections with vigorous levels of exercise. See Heath et al., 1992 Sports Medicine 14(6) 353-365. -3- [0014] In addition to physical activity and exercise, stress can be evinced by external factors such as trauma (physical), major life events, physical health status and lifestyle. The way in which these external factors are perceived and the way in which the body adjusts influence the ultimate physiological response. The body's response to stress is handled by an 5 allostatic system (adaptive) consisting primarily of the sympathetic nervous system and the hypothalamic, pituitary, adrenal axis (HPA axis) (McEwen B. 1998, New England Journal of Medicine, 338:171-179). The term "allostatic load" refers to the amount of physiological response resulting from the balance between the initiation of a complex response and the shutting down of this response. Allostatic load can result from frequent stress, lack of adaptation 10 to stress, inability to turn off an allostatic response, and lack of allostatic response in one system resulting in an increased response in another. [0015] There is strong evidence to suggest that allostatic load leads to increased susceptibility to disease, risk of contracting disease and increased disease incidence. For example, stress induced increases in blood pressure can trigger myocardial infarction in humans 15 and atherosclerosis in primates (Muller et al., 1989 Circulation 79:733-743, and Kaplan et al., 1991 Circulation, 84 Suppl VI:VI-23-VI-32,). Intense athletic training increases allostatic load resulting in weight loss, amenorrhoea and anorexia nervosa (Boyar et-al., 1977 New Engl J Med. 296:190-193, and Loucks et al., 1989 J Clin. Endocrinol. Metabol. 68:402-411). Repeated social defeat (stressor) in mice is associated with (amongst other findings) increased plasma 20 concentrations of corticosterone, which is a known immunosuppressant (Stark et al., Am. J. Physiol. Regul. Integrr. Comp. Physiol. 280: RI 799-RI 805). Age is correlated with the ability to turn off the HPA axis, and prolonged stimulation of physiological systems through the HPA axis can result in hippocampus damage and consequent cognitive deficits (Lupien et al., 1994 J Neurosci. 14:2893-2903). In Lewis rats, genetically determined to have hyporesponsiveness of 25 the HPA axis, increased inflammatory responses result in an increased incidence of autoimmune and inflammatory disturbances (Sternburg et al., 1989 Proc. Natl. Acad. Sci (USA) 86: 4771 4775). Low HPA responsiveness is also considered to be involved in human fibromyalgia (Crofford et al., 1994 Arthritis Rheum. 37:1583-1592), chronic fatigue syndrome (Poteliakhoff A. 1981 JPsychosom. Res. 25:91-95), infant atopic dermatitis (Buske-Kirschbaum et al., 1997 30 Psychosom med. 59:419-426) and post-traumatic stress disorder (Yehuda et al., 1991 Bio. Psychiatry 30:1031-1048). 100161 Approximating allostatic load has been attempted by using measures of metabolic and cardiovascular physiology including, systolic blood pressure, overnight urinary cortisol and catecholamine excretion, ratio of waist to hip measurement, glycosylated 35 hemoglobin value, ratio of serum high density lipoprotein in the total serum cholesterol concentration, serum concentration of dehydroepiandrosterone sulfate, and serum concentration of high density lipoprotein cholesterol. Patients with a lower allostatic score from measuring -4these parameters had higher physical and mental functioning and a lower incidence of cardiovascular disease, hypertension and diabetes (Seeman et al., 1997 Arch. Intern. Med. 157:2259-2268). High serum fibrinogen concentrations have also been correlated to increased risk of coronary heart disease (Markowe et al., 1985 British Med. J. 291:1312-1314). In 5 addition it has been noted that stress induces atrophy of the pyramidal neurones in the CA3 region of the hippocampus that can be detected using magnetic resonance imaging (Sapolsky R. M. 1996 Science 273:749-750.). These measures require multiple separate assays, are expensive and often laborious, and only provide an approximation of allostatic load. [00171 In summary there is a need for more effective processes for measuring 10 allostatic load. [0018] It is well known that stress affects the immune system (Hawkley and Cacioppo, 2004 Brain Behav. Imm. 18:114-119; Engler et al., 2004 JNeuroimm. 148:106-115; Woods et al., 2003 Brain Behav. Imm. 17: 384-392; Mars et al., 1998 Biochem Biophys. Res. Comm. 249: 366-370; Bierhaus et al.,, 2003 Proc. Nati. Acad Sci (USA) 100(4):1920-1925; 15 Horohov et al., 1996 Vet Immunol. Immunopath. 53:221-233). Stress acts on the immune system mainly through the sympathetic nervous system and HPA axis causing the release of catecholamines, corticotrophin and cortisol (an example of a steroid). These molecules have known immunomodulatory effects but their mechanism of action is not fully understood. For example, glucocorticoids (steroids) such as cortisol bind to steroid receptors on the outside of 20 cells and are then transported directly to the cell nucleus. Once inside the nucleus, steroid hormones can modulate gene expression, and hence immune function, through steroid responsive elements upstream of gene coding regions (Geng and Vedeckis, 2004 Mol. Endocrinol. 18(4):912-924). For the purposes of its effects on the immune system, stress can be classified into acute (once over a period of less than say two days) and chronic forms (persistent 25 stress over a period of several days or months). Acute stress has been demonstrated to enhance the immune system by redistributing white blood cells from blood to various body compartments such as the skin, lymph nodes and bone marrow (Dhabhar et al., 1995 J. Immunol. 154:5511-5527) the effect of which is partly due to release of endogenous glucocorticoids. The affect of acute stress has been reported to last for 3-5 days (Dhabhar et al., 30 1996 Jlmmunol. 157:1638-1644.). On the other hand, chronic stress elicits the HPA axis and the autonomic nervous system and reduces cellular immune responses and increases susceptibility to disease (McEwen et al., 1997 Brain Res. Rev. 23:79-113; Cohen et al., 1992 Psychol. Sci. 3:301-304; Cohen et al., 1993 JAMA, 277:1940-1944; Peijie et al., 2003 Life Sciences 72:2255-2262). 35 [0019] In summary, there is a need for better modalities for measuring and monitoring the effects of allostatic load on the function of the immune system. -5- SUMMARY OF THE INVENTION [00201 The present invention represents a significant advance over current technologies for quantifying allostatic load and for measuring and monitoring immune function. It is predicated in part on measuring the level of certain functional markers in cells, especially 5 circulating leukocytes, of the host. More particularly, the present invention relates to molecules and assays, which are useful in screening and monitoring animals for the presence or risk of developing disease or illness through immune system dysfunction as a result of stress, in determining the ability of an animal to cope with, or adapt to, external stressors, and in monitoring immune function when administering immune-modulating drugs. The invention has 10 practical use in monitoring animals under stress, especially those in athletic training, in measuring the effects of aging on the ability to respond to external stressors, and in enabling better treatment and management decisions to be made in animals at risk of exposure to disease, or susceptible to disease through the effects of stress. In certain embodiments, the invention has practical applications in measuring the response to vaccination or immune-modifying therapies, 15 for example, in animals under stress, which may not develop an appropriate protective response to vaccination or therapy. In other embodiments, the invention has practical use in monitoring the immune response to natural disease when an animal is subject to stressful conditions or at risk due to inappropriate response to stress. This represents a significant and unexpected advance in the screening, monitoring and management of animals under stress. 20 [0021] Thus, the present invention addresses the problem of detecting the presence, absence or degree of a physiological stress response or of assessing well being including the function of the immune system by detecting, for example, a differential gene expression pattern that may be measured in host cells. Advantageous embodiments involve monitoring the expression of certain genes in peripheral leukocytes of the immune system, which may be 25 reflected in changing patterns of RNA levels or protein production that correlate with allostatic stress load or with an immune-modulating event. 100221 Accordingly, in one aspect, the present invention provides methods for determining the presence or degree of a physiological response to stress or a related condition in a test subject. These methods generally comprise detecting in the subject aberrant expression of 30 at least one gene (also referred to herein as a "stress marker gene") selected from the group consisting of: (a) a gene comprising a nucleotide sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth in any one of SEQ D NO: 1, 3, 4, 5, 7, 9, 11, 13, 15, 16, 17, 19, 21, 23, 24, 25, 26, 28, 29, 30, 32, 33, 34, 35, 37, 38, 39, 40, 41, 42, 44, 46, 48, 50, 51, 52, 54, 55, 56, 57, 59, 62, 63, 35 64, 66, 68, 70, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 90, 91, 92, 93, 95, 96, 97, 99, 101, 103, 105, 107, 108, 109, 111, 113, 115, 117, 118, 119, 121, 123, 125, 126, 127, 129, 130, 131, 133, -6- 135, 137, 139, 141, 143, 144, 145, 147, 148, 150, 151, 153, 155, 156, 158, 160, 161, 163, 164, 165, 167, 169, 170, 171, 173, 175, 176, 178, 180, 182, 184, 185, 186, 187, 188, 190, 192, 194, 195, 196, 198, 200, 202, 204, 206, 208, 210, 212, 214, 216, 218, 220, 222, 224, 226, 228, 230, 232, 233, 234, 236, 238, 239, 240, 241, 242, 243, 244, 246 or 248, or a complement thereof; (b) 5 a gene comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120,122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193,197, 199, 201, 203, 205, 207, 10 209,211,213, 215, 217,219, 221, 223, 225, 227,229, 231,235, 237, 245, 247 or 249; (c) a gene comprising a nucleotide sequence that encodes a polypeptide that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with at least a portion of the sequence set forth in SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 15 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249, wherein the portion comprises at least 15 contiguous amino acid residues of that sequence; and (d) a gene comprising a nucleotide sequence that hybridizes to the sequence of (a), (b), (c) or a 20 complement thereof, under at least low, medium or high stringency conditions. In accordance with the present invention, these stress marker genes are aberrantly expressed in animals with a physiological response to stress or with an allostatic load. Suitably, the related condition is immunodepression. [0023] Suitably, the presence of the physiological response to stress or related 25 condition is associated with psychological stress or physical stress (e.g., physical duress such as athletic training and physical trauma). Illustrative psychological conditions include depression, generalized anxiety disorder, post traumatic stress disorder, panic, chronic fatigue, myalgic encephalopathy, stress through restraint, sleep deprivation, overeating and behavioral (operant) conditioning. Other psychological conditions, especially relating to veterinary applications, 30 include, but are not limited to, stress related to confinement, sheering, shipping or human animal interaction. Illustrative examples of physical stress include physical duress such as athletic training and physical trauma. [0024] As used herein, polynucleotide expression products of stress marker genes are referred to as "stress marker polynucleotides." Polypeptide expression products of the stress 35 marker genes are referred to herein as "stress marker polypeptides." -7- [0025] Thus, in some embodiments, the methods comprise detecting aberrant expression of a stress marker polynucleotide selected from the group consisting of (a) a polynucleotide comprising a nucleotide sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth 5 in any one of SEQ ID NO: 1, 3, 4, 5, 7, 9, 11, 13, 15, 16, 17, 19, 21, 23, 24, 25, 26, 28, 29, 30, 32, 33, 34, 35, 37, 38, 39, 40, 41, 42,44, 46, 48, 50, 51, 52, 54, 55, 56, 57, 59, 62, 63, 64, 66, 68, 70, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 90,91, 92, 93, 95, 96, 97, 99, 101,103, 105, 107, 108, 109, 111, 113, 115, 117, 118, 119, 121, 123, 125, 126, 127, 129, 130, 131, 133, 135, 137, 139, 141, 143, 144, 145, 147, 148, 150, 151, 153, 155, 156, 158, 160, 161, 163, 164, 165, 167, 10 169, 170, 171, 173, 175, 176, 178, 180, 182, 184, 185, 186, 187, 188, 190, 192, 194, 195, 196, 198, 200, 202, 204, 206, 208, 210, 212, 214, 216, 218, 220, 222, 224, 226, 228, 230, 232, 233, 234, 236, 238, 239, 240, 241, 242, 243, 244, 246 or 248, or a complement thereof; (b) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 15 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249; (c) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide that shares at 20 least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with at least a portion of the sequence set forth in SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27,.31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67,69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94,98, 100, 102, 104, 106, 110, 112,114,116,120,122,124, 128, 132,134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 25 197, 199,201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249, wherein the portion comprises at least 15 contiguous amino acid residues of that sequence; and (d) a polynucleotide comprising a nucleotide sequence that hybridizes to the sequence of (a), (b), (c) or a complement thereof, under at least low stringency conditions. [0026] In other embodiments, the methods comprise detecting aberrant expression 30 of a stress marker polypeptide selected from the group consisting of: (i) a polypeptide comprising an amino acid sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with the sequence set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 35 122, 124,128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249; (ii) a polypeptide comprising a -8portion of the sequence set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177; 179, 181, 183, 189, 191, 193, 197, 199, 201, 5 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249, wherein the portion comprises at least 5 contiguous amino acid residues of that sequence; (iii) a polypeptide comprising an amino acid sequence that shares at least 30% (and at least 31% to at least 99% and all integer percentages in between) similarity with at least 15 contiguous amino acid residues of the sequence set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 10 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249; and (iv) a polypeptide comprising a portion of the sequence set forth in 15 any one of SEQ ID NO: 2, 6, 8, 10,12,14, 18, 20, 22,27, 31, 36, 43, 45, 47,49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154,157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249, wherein the portion 20 comprises at least 5 contiguous amino acid residues of that sequence and is immuno-interactive with an antigen-binding molecule that is immuno-interactive with a sequence of (i), (ii) or (iii). [0027] Typically, aberrant expression of a stress marker gene is detected by: (1) measuring in a biological sample obtained from the subject the level or functional activity of an expression product of at least one stress marker gene and (2) comparing the measured level or 25 functional activity of each expression product to the level or functional activity of a corresponding expression product in a reference sample obtained from one or more normal subjects or from one or more subjects not under stress, wherein a difference in the level or functional activity of the expression product in the biological sample as compared to the level or functional activity of the corresponding expression product in the reference sample is indicative 30 of the presence of a physiological response to stress. In some embodiments, the method further comprises determining the degree of stress response (or stress level) or the degree of immunomodulation when the measured level or functional activity of the or each expression product is different than the measured level or functional activity of the or each corresponding expression product. In these embodiments, the difference typically represents an at least about 35 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80% or 90%, or even an at least about 100%, 200%, 300%, 400%, 500%, 600%, 700%, 800%, 900% or 1000% increase, or an at least about 10%, 20%, 30% 40%, 50%, 60%, 70%, 80%, 90%, 92%, 94%, 96%, 97%, 98% or 99%, or even an at -9least about 99.5%, 99.9%, 99.95%, 99.99%, 99.995% or 99.999% decrease in the level or functional activity of an individual expression product as compared to the level or function activity of an individual corresponding expression product. , which is hereafter referred to as "aberrant expression." In illustrative examples of this type, the presence of a physiological 5 response to stress is determined by detecting a decrease in the level or functional activity of at least one stress marker polynucleotide selected from (a) a polynucleotide comprising a nucleotide sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth in any one of SEQ ID NO: 1, 3, 4, 7, 9, 11, 19, 21, 24, 25, 33, 34, 38, 39, 40, 41, 42, 50, 51, 56, 57, 59, 62, 63, 66, 70, 10 71, 73, 75, 79, 81, 83, 89, 90, 91, 92, 93, 97, 99, 105, 107, 108, 111, 119, 121, 122, 123, 129, 130, 137, 139, 140, 141, 142, 143 or 185, or a complement thereof; (b) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 2, 8, 10, 12, 20, 22, 43, 58, 60, 67, 71, 72, 74, 76, 80, 82, 84, 94, 98, 100, 106, 112, 120, 122, 123, 124 or 138; (c) a polynucleotide comprising a 15 nucleotide sequence that encodes a polypeptide that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with at least a portion of the sequence set forth in SEQ ID NO: 2, 8, 10, 12, 20, 22, 43, 58, 60, 67, 71, 72, 74, 76, 80, 82, 84, 94, 98, 100, 106,.112, 120, 122, 123, 124 or 138, wherein the portion comprises at least 15 contiguous amino acid residues of that sequence; and (d) a polynucleotide comprising a 20 nucleotide sequence that hybridizes to the sequence of (a), (b), (c) or a complement thereof, under at least low, medium, or high stringency conditions. [00281 In other illustrative examples, the presence of a physiological response to stress is determined by detecting an increase in the level or functional activity of at least one stress marker polynucleotide selected from (a) a polynucleotide comprising a nucleotide 25 sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth in any one of SEQ ID NO: 5, 13, 15, 16, 17, 23, 26, 28, 29, 30, 32, 35, 37, 44, 46, 48, 52, 54, 55, 64, 68, 77, 85, 87, 95, 96, 101, 103, 113, 115, 117, 118, 125, 126, 131, 133, 135, 144, 145, 147, 148, 150, 151, 153, 155, 156, 158, 160, 161, 163, 164, 165, 167, 169, 170, 171, 173, 175, 176, 178, 180, 182, 183, 184, 186, 187, 30 188, 190, 192, 194, 195, 196, 198, 200, 202, 204,206 or 210, or a complement thereof; (b) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 6, 14, 18, 27, 31, 36, 45, 47, 49, 53, 65, 69, 78, 86, 88, 102, 104, 114, 116, 132, 134, 136, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 189, 191, 193, 197, 199, 201, 203, 205, 207 or 211; (c) a 35 polynucleotide comprising a nucleotide sequence that encodes a polypeptide that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with at least a portion of the sequence set forth in SEQ ID NO: 6, 14, 18, 27, 31, 36, -10- 45, 47, 49, 53, 65, 69, 78, 86, 88, 102, 104, 114, 116, 132, 134, 136, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 189, 191, 193, 197, 199, 201, 203, 205, 207 or 211, wherein the portion comprises at least 15 contiguous amino acid residues of that sequence; and (d) a polynucleotide comprising a nucleotide sequence that hybridizes to the sequence of (a), 5 (b), (c) or a complement thereof, under at least low, medium, or high stringency conditions. [0029] In some embodiments, the method further comprises determining the absence of a physiological response to stress when the measured level or functional activity of the or each expression product is the same as or similar to the measured level or functional activity of the or each corresponding expression product. In these embodiments, the measured 10 level or functional activity of an individual expression product varies from the measured level or functional activity of an individual corresponding expression product by no more than about 20%, 18%, 16%, 14%, 12%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1% or 0.1%, which is hereafter referred to as "normal expression." [0030] In some embodiments, the methods comprise measuring the level or 15 functional activity of individual expression products of at least about 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45 stress marker genes. For example, the methods may comprise measuring the level or functional activity of a stress marker polynucleotide either alone or in combination with as much as 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 20 30, 29,28, 27, 26, 25, 24, 23, 22,21, 20, 19, 18, 17, 16, 15, 14,13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 other stress marker polynucleotide(s). In another example, the methods may comprise measuring the level or functional activity of a stress marker polypeptide either alone or in combination with as much as 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 30, 29, 28, 27, 26, 25, 24, 23, 22, 21, 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 other 25 stress marker polypeptides(s). In illustrative examples of this type, the methods comprise measuring the level or functional activity of individual expression products of at least 1, 2, 3, 4, 5 or 6 stress marker genes that have a very high correlation with the presence or risk of a physiological response to stress (hereafter referred to as "level one correlation stress marker genes"), representative examples of which include, but are not limited to, (a) a polynucleotide 30 comprising a nucleotide sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth in any one of SEQ ID NO: 89, 90, 103, 125, 126, 163, 178, 182, 184 or 190, or a complement thereof; (b) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 104, 179, 183 or 189; (c) a 35 polynucleotide comprising a nucleotide sequence that encodes a polypeptide that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with at least a portion of the sequence set forth in SEQ ID NO: 104, 179, 183 or 189, -11 wherein the portion comprises at least 15 contiguous amino acid residues of that sequence; and (d) a polynucleotide comprising a nucleotide sequence that hybridizes to the sequence of (a), (b), (c) or a complement thereof, under at least low, medium, or high stringency conditions. [0031] In other illustrative examples, the methods comprise measuring the level or 5 functional activity of individual expression products of at least 1, 2, 3, 4, 5, 6, 7 or 8 stress marker genes that have a high correlation with the presence or risk of a physiological response to stress (hereafter referred to as "level two correlation stress marker genes"), representative examples of which include, but are not limited to, (a) a polynucleotide comprising a nucleotide sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in 10 between) sequence identity with the sequence set forth in any one of SEQ ID NO: 17, 23, 44, 52, 133, 135, 144, 147, 148, 151, 155, 192, 196, 202 or 206, or a complement thereof; (b) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 18, 20, 45, 53, 134, 136, 149, 152, 193, 197 or 207; (c) a polynucleotide comprising a nucleotide sequence that encodes a 15 polypeptide that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with at least a portion of the sequence set forth in SEQ ID NO: 18, 20, 45, 53, 134, 136, 149, 152, 193, 197 or 207, wherein the portion comprises at least 15 contiguous amino acid residues of that sequence; and (d) a polynucleotide comprising a nucleotide sequence that hybridizes to the sequence of (a), (b), (c) or a complement thereof, 20 under at least low, medium, or high stringency conditions. [0032] In still other illustrative examples, the methods comprise measuring the level or functional activity of individual expression products of at least 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 stress marker genes that have a medium correlation with the presence or risk of a physiological response to stress (hereafter referred to as "level three correlation stress marker genes"), 25 representative examples of which include, but are not limited to, (a) a polynucleotide comprising a nucleotide sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth in any one of SEQ ID NO: 5, 30, 37, 48, 54, 55, 64, 66, 70, 77, 79, 85, 91, 92, 95, 96, 101, 115, 117, 118, 121, 150, 153, 158, 164, 170, 180, 186 or198, or a complement thereof; (b) a polynucleotide 30 comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 6, 31, 49, 65, 67, 78, 80, 86, 102, 116, 122, 154, 159, 181 or 199; (c) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with at least a portion of the sequence set forth in SEQ ID NO: 35 6, 31, 49, 65, 67, 78, 80, 86, 102, 116, 122, 154, 159, 181 or 199, wherein the portion comprises at least 15 contiguous amino acid residues of that sequence; and (d) a polynucleotide -12comprising a nucleotide sequence that hybridizes to the sequence of (a), (b), (c) or a complement thereof, under at least low, medium, or high stringency conditions. [00331 In still other illustrative examples, the methods comprise measuring the level or functional activity of individual expression products of at least 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 5 stress marker genes that have a moderate correlation with the presence or risk of a physiological response to stress (hereafter referred to as "level four correlation stress marker genes"), representative examples of which include, but are not limited to, (a) a polynucleotide comprising a nucleotide sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth in any one of 10 SEQ ID NO: 7, 15, 16, 19, 21, 24, 25, 26, 28, 35, 38, 39, 42, 46, 57, 68, 73, 81, 83,.97, 99, 107, 113, 123, 160, 165, 175, 187, 188, 194, 195 or 2 0 0 , or a complement thereof; (b) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 20, 22, 27, 29, 36, 42, 43, 58, 69, 74, 82, 84, 98, 100, 108, 114, 124, 166, 189 or 201; (c) a polynucleotide comprising a nucleotide 15 sequence that encodes a polypeptide that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with at least a portion of the sequence set forth in SEQ ID NO: 20, 22, 27, 29, 36, 42, 43, 58, 69, 74, 82, 84, 98, 100, 108, 114, 124, 166, 189 or 201, wherein the portion comprises at least 15 contiguous amino acid residues of that sequence; and (d) a polynucleotide comprising a nucleotide sequence that 20 hybridizes to the sequence of (a), (b), (c) or a complement thereof, under at least low, medium, or high stringency conditions. [0034] In still other illustrative examples, the methods comprise measuring the level or functional activity of individual expression products of at least 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 stress marker genes that have a lower correlation with the presence or risk of a physiological 25 response to stress (hereafter referred to as "level five correlation stress marker genes"), representative examples of which include, but are not limited to, (a) a polynucleotide comprising a nucleotide sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth in any one of SEQ ID NO: 1, 3, 9, 11, 13, 32, 33, 34, 40, 41, 50, 51, 56, 59, 62, 63, 71, 75, 87, 93, 105, 111, 30 119, 127, 129, 130,131, 137, 139, 141, 143, 145, 156, 161, 167, 169, 171, 173, 176, 1 8 5, 204 or 210, or a complement thereof; (b) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 2, 4, 12, 14, 60, 61, 72, 76, 88, 94, 106, 112, 120, 128, 132, 138, 140, 142, 146, 157, 162, 168, 172, 174, 177, 205 or 211; (c) a polynucleotide comprising a nucleotide sequence that encodes a 35 polypeptide that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with at least a portion of the sequence set forth in SEQ ID NO: 2, 4, 12, 14, 60, 61, 72, 76, 88, 94, 106, 112, 120, 128, 132, 138, 140, 142, 146, 157, 162, 168, -13 - 172, 174, 177, 205 or 211, wherein the portion comprises at least 15 contiguous amino acid residues of that sequence; and (d) a polynucleotide comprising a nucleotide sequence that hybridizes to the sequence of (a), (b), (c) or a complement thereof, under at least low, medium, or high stringency conditions. 5 [0035] In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level one correlation stress marker gene. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level one correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression 10 product of at least 1 level one correlation stress marker gene and the level or functional activity of an expression product of at least 1 level two stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level one correlation stress marker genes and the level or functional activity of an expression product of at least 1 level two correlation stress marker gene. In still other 15 embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level one correlation stress marker gene and the level or functional activity of an expression product of at least 2 level two correlation stress marker genes. [0036] In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level one correlation stress marker gene 20 and the level or functional activity of an expression product of at least I level three correlation stress marker gene. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level one correlation stress marker genes and the level or functional activity of an expression product of at least I level three correlation stress marker gene. In still other embodiments, the methods comprise measuring the 25 level or functional activity of an expression product of at least 1 level one correlation stress marker gene and the level or functional activity of an expression product of at least 2 level three correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level one correlation stress marker gene and the level or functional activity of an expression product of at least 3 level three 30 correlation stress marker genes. [0037] In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level one correlation stress marker gene and the level or functional activity of an expression product of at least 1 level four correlation stress marker gene. In other embodiments, the methods comprise measuring the level or 35 functional activity of an expression product of at least 2 level one correlation stress marker genes and the level or functional activity of an expression product of at least 1 level four -14correlation stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level one correlation stress marker gene and the level or functional activity of an expression product of at least 2 level four correlation stress marker gene. In still other embodiments, the methods comprise measuring the 5 level or functional activity of an expression product of at least I level one correlation stress marker gene and the level or functional activity of an expression product of at least 3 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level one correlation stress marker gene and the level or functional activity of an expression product of at least 4 level four 10 correlation stress marker genes. [00381 In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level one correlation stress marker gene and the level or functional activity of an expression product of at least I level five correlation stress marker gene. In other embodiments, the methods comprise measuring the level or 15 functional activity of an expression product of at least 2 level one correlation stress marker genes and the level or functional activity of an expression product of at least I level five correlation stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level one correlation stress marker gene and the level or functional activity of an expression product of at least 2 level five 20 correlation stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level one correlation stress marker gene and the level or functional activity of an expression product of at least 3 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level one correlation stress 25 marker gene and the level or functional activity of an expression product of at least 4 level five correlation stress marker genes. [00391 In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress marker gene. In other embodiments, the methods comprise measuring the level or functional activity of 30 an expression product of at least 2 level two correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level two correlation stress marker gene and the level or functional activity of an expression product of at least 1 level three correlation stress marker gene. In other embodiments, the methods comprise measuring the level or functional activity of an expression 35 product of at least 2 level two correlation stress marker genes and the level or functional activity of an expression product of at least 1 level three correlation stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression . ..15 product of at least 1 level two correlation stress marker gene and the level or functional activity of an expression product of at least 2 level three correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress marker gene and the level or functional activity 5 of an expression product of at least 3 level three correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress marker gene and the level or functional activity of an expression product of at least 4 level three correlation stress marker genes. 100401 In some embodiments, the methods comprise measuring the level or 10 functional activity of an expression product of at least 1 level two correlation stress marker gene and the level or functional activity of an expression product of at least 1 level four correlation stress marker gene. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level two correlation stress marker genes and the level or functional activity of an expression product of at least 1 level four 15 correlation stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress marker gene and the level or functional activity of an expression product of at least 2 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress 20 marker gene and the level or functional activity of an expression product of at least 3 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress marker gene and the level or functional activity of an expression product of at least 4 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the 25 level or functional activity of an expression product of at least I level two correlation stress marker gene and the level or functional activity of an expression product of at least 5 level four correlation stress marker genes. 100411 In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress marker 30 gene. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level two correlation stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress marker gene and the level or functional activity of an expression product of at least I level five correlation stress marker gene. In other 35 embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level two correlation stress marker genes and the level or functional activity of an expression product of at least 1 level five correlation stress marker gene. In still other -16embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level two correlation stress marker gene and the level or functional activity of an expression product of at least 2 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression 5 product of at least 1 level two correlation stress marker gene and the level or functional activity of an expression product of at least 3 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress marker gene and the level or functional activity of an expression product of at least 4 level five correlation stress marker genes. In still other 10 embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level two correlation stress marker gene and the level or functional activity of an expression product of at least 5 level five correlation stress marker genes. 100421 In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level three correlation stress marker 15 gene. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level three correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level three correlation stress marker gene and the level or functional activity of an expression product of at least 1 level four correlation stress marker gene. In other 20 embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level three correlation stress marker genes and the level or functional activity of an expression product of at least 1 level four correlation stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level three correlation stress marker gene and the level or 25 functional activity of an expression product of at least 2 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level three correlation stress marker gene and the level or functional activity of an expression product of at least 3 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or 30 functional activity of an expression product of at least 1 level three correlation stress marker gene and the level or functional activity of an expression product of at least 4 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level three correlation stress marker gene and the level or functional activity of an expression product of at least 5 level four 35 correlation stress marker genes. [0043] In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level three correlation stress marker -17gene and the level or functional activity of an expression product of at least 1 level five correlation stress marker gene. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level three correlation stress marker genes and the level or functional activity of an expression product of at least 1 level five 5 correlation stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level three correlation stress marker gene and the level or functional activity of an expression product of at least 2 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level three correlation stress 10 marker gene and the level or functional activity of an expression product of at least 3 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level three correlation stress marker gene and the level or functional activity of an expression product of at least 4 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the 15 level or functional activity of an expression product of at least I level three correlation stress marker gene and the level or functional activity of an expression product of at least 5 level five correlation stress marker genes. [00441 In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level four correlation stress marker 20 gene. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level four correlation stress marker genes. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 3 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 25 3 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 4 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 5 level four correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or 30 functional activity of an expression product of at least 6 level four correlation stress marker genes. [0045] In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level four correlation stress marker gene and the level or functional activity of an expression product of at least 1 level five 35 correlation stress marker gene. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 2 level four correlation stress marker genes and the level or functional activity of an expression product of at least 1 level five -18 correlation stress marker gene. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level four correlation stress marker gene and the level or functional activity of an expression product of at least 2 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the 5 level or functional activity of an expression product of at least 1 level four correlation stress marker gene and the level or functional activity of an expression product of at least 3 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level four correlation stress marker gene and the level or functional activity of an expression product of at least 4 level five 10 correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level four correlation stress marker gene and the level or functional activity of an expression product of at least 5 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least I level four correlation stress 15 marker gene and the level or functional activity of an expression product of at least 6 level five correlation stress marker genes. [0046] In some embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 1 level five correlation stress marker gene. In other embodiments, the methods comprise measuring the level or functional activity of 20 an expression product of at least 2 level five correlation stress marker genes. In other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 3 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 3 level five correlation stress marker genes. In still other embodiments, the methods comprise 25 measuring the level or functional activity of an expression product of at least 4 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 5 level five correlation stress marker genes. In still other embodiments, the methods comprise measuring the level or functional activity of an expression product of at least 6 level five correlation stress marker 30 genes. [00471 Advantageously, the biological sample comprises blood, especially peripheral blood, which typically includes leukocytes. Suitably, the expression product is selected from a RNA molecule or a polypeptide. In some embodiments, the expression product is the same as the corresponding expression product. In other embodiments, the expression 35 product is a variant (e.g., an allelic variant) of the corresponding expression product. -19- 10048] In certain embodiments, the expression product or corresponding expression product is a target RNA (e.g., mRNA) or a DNA copy of the target RNA whose level is measured using at least one nucleic acid probe that hybridises under at least low stringency conditions to the target RNA or to the DNA copy, wherein the nucleic acid probe comprises at 5 least 15 contiguous nucleotides of a stress marker gene. In these embodiments, the measured level or abundance of the target RNA or its DNA copy is normalised to the level or abundance of a reference RNA or a DNA copy of the reference RNA that is present in the same sample. Suitably, the nucleic acid probe is immobilized on a solid or semi-solid support. In illustrative examples of this type, the nucleic acid probe forms part of a spatial array of nucleic acid probes. 10 In some embodiments, the level of nucleic acid probe that is bound to the target RNA or to the DNA copy is measured by hybridization (e.g., using a nucleic acid array). In other embodiments, the level of nucleic acid probe that is bound to the target RNA or to the DNA copy is measured by nucleic acid amplification (e.g., using a polymerase chain reaction (PCR)). In still other embodiments, the level of nucleic acid probe that is bound to the target RNA or to 15 the DNA copy is measured by nuclease protection assay. [0049] In other embodiments, the expression product or corresponding expression product is a target polypeptide whose level is measured using at least one antigen-binding molecule that is immuno-interactive with the target polypeptide. In these embodiments, the measured level of the target polypeptide is normalized to the level of a reference polypeptide 20 that is present in the same sample. Suitably, the antigen-binding molecule is immobilized on a solid or semi-solid support. In illustrative examples-of this type, the antigen-binding molecule forms part of a spatial array of antigen-binding molecule. In some embodiments, the level of antigen-binding molecule that is bound to the target polypeptide is measured by immunoassay (e.g., using an ELISA). 25 [00501 In still other embodiments, the expression product or corresponding expression product is a target polypeptide whose level is measured using at least one substrate for the target polypeptide with which it reacts to produce a reaction product. In these embodiments, the measured functional activity of the target polypeptide is normalized to the functional activity of a reference polypeptide that is present in the same sample. 30 [00511 In some embodiments, a system is used to perform the method, which suitably comprises at least one end station coupled to a base station. The base station is suitably caused (a) to receive subject data from the end station via a communications network, wherein the subject data represents parameter values corresponding to the measured or normalized level or functional activity of at least one expression product in the biological sample, and (b) to 35 compare the subject data with predetermined data representing the measured or normalized level or functional activity of at least one corresponding expression product in the reference sample to -20thereby determine any difference in the level or functional activity of the expression product in the biological sample as compared to the level or functional activity of the corresponding expression product in the reference sample. Desirably, the base station is further caused to provide a diagnosis for the presence, absence, degree, or risk of development, of a stress 5 response. In these embodiments, the base station may be further caused to transfer an indication of the diagnosis to the end station via the communications network. [00521 In another aspect, the invention provides methods for determining the presence or degree of immunosuppression in a test subject. These methods generally comprise detecting in the subject aberrant expression of at least one stress marker gene as broadly 10 described above. [0053] In yet another aspect, the present invention provides methods for treating or preventing the development of stress or a related condition in a test subject. These methods generally comprise detecting aberrant expression of at least one stress marker gene in the subject, and managing the environment of the subject to prevent or minimize exposure of the 15 subject to a causative stressor and/or administering to the subject an effective amount of an agent that treats or ameliorates the symptoms or reverses or inhibits the development of stress in the subject. In certain embodiments, the related condition is immunosuppression. [0054] Accordingly, in a related aspect, the present invention provides methods for treating or preventing the development of immunosuppression in a test subject. These methods 20 generally comprise detecting aberrant expression of at least one stress marker gene in the subject, and managing the environment of the subject to prevent or minimize exposure of the subject to a causative stressor and/or administering to the subject an effective amount of an agent that treats or ameliorates the symptoms or reverses or inhibits the development of stress in the subject. 25 [0055] In still another aspect, the present invention provides methods for assessing the capacity of a subject's immune system to produce an immunogenic response to a selected antigen. These methods generally comprise determining whether at least one stress marker gene as broadly described above is normally or aberrantly expressed in the subject, whereby normal expression of the or each stress marker gene is indicative of a normal capacity to produce the 30 immunogenic response and whereby aberrant expression of the or each stress marker gene is indicative of an impaired capacity to produce the immunogenic response. [0056] In a further aspect, the present invention provides methods for eliciting an immune response to a selected antigen in a test subject via administration of a composition comprising the antigen. These methods generally comprise detecting normal expression of at 35 least one stress marker gene as broadly described above in the subject and administering the composition to the subject. -21 - [0057] In some embodiments, the methods further comprise detecting in the subject aberrant expression of at least one stress marker gene as broadly described above and managing the environment of the subject to prevent or minimize exposure of the subject to a causative stressor and/or administering to the subject an effective amount of an agent that reverses or 5 inhibits the development of stress in the subject, and administering the composition to the subject. In some embodiments, the composition is administered to the subject when the or each stress marker gene is normally expressed in the subject. [00581 In a related aspect, the invention provides methods for improving an immune response to a selected antigen in a test subject to whom/which has been administered a 10 composition comprising the antigen. These methods generally comprise detecting aberrant expression of at least one stress marker gene as broadly described above in the subject and managing the environment of the subject to prevent or minimize exposure of the subject to a causative stressor and/or administering to the subject an effective amount of an agent that reverses or inhibits the development of stress in the subject, whereby the management or 15 administration leads to normal expression of the or each stress marker gene in the subject. 100591 In another aspect, the present invention provides isolated polynucleotides, referred to herein as "stress marker polynucleotides," which are generally selected from: (a) a polynucleotide comprising a nucleotide sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth 20 in any one of SEQ ID NO: 15, 16, 23, 24, 25, 28, 29, 32, 33, 34, 37, 38, 39, 40, 41, 50, 51, 54, 55, 62, 63, 89, 90, 91, 92, 95, 96, 107, 108, 117, 118, 125, 126, 129, 130, 143, 144, 147, 150, 155, 163, 164, 169, 170, 175, 184, 185, 186, 187, 194, 195, 232, 233, 238, 239, 240, 241, 242 or 243, or a complement thereof; (b) a polynucleotide comprising a portion of the sequence set forth in any one of SEQ ID NO: 15, 16, 23, 24, 25, 28, 29, 32, 33, 34, 37, 38, 39, 40, 41, 50, 51, 25 54, 55, 62, 63, 89, 90, 91, 92, 95, 96, 107, 108, 117, 118, 125, 126, 129, 130, 143, 144, 147, 150, 155, 163, 164, 169, 170, 175, 184, 185, 186, 187, 194, 195, 232, 233, 238, 239, 240, 241, 242 or 243, or a complement thereof, wherein the portion comprises at least 15 contiguous nucleotides of that sequence or complement; (c) a polynucleotide that hybridizes to the sequence of (a) or (b) or a complement thereof, under at least low, medium or high stringency 30 conditions; and (d) a polynucleotide comprising a portion of any one of SEQ ID NO: 15, 16, 23, 24, 25, 28, 29, 32, 33, 34, 37, 38, 39, 40, 41, 50, 51, 54, 55, 62, 63, 89, 90, 91, 92, 95, 96, 107, 108, 117, 118, 125, 126, 129, 130, 143, 144, 147, 150, 155, 163, 164, 169, 170, 175, 184, 185, 186, 187, 194, 195, 232, 233, 238, 239, 240, 241, 242 or 243, or a complement thereof, wherein the portion comprises at least 15 contiguous nucleotides of that sequence or complement and 35 hybridizes to a sequence of (a), (b) or (c), or a complement thereof, under at least low, medium or high stringency conditions. -22 - [00601 In another aspect, the present invention provides a nucleic acid construct comprising a polynucleotide as broadly described above in operable connection with a regulatory element, which is operable in a host cell. In certain embodiments, the construct is in the form of a vector, especially an expression vector. 5 [0061] In yet another aspect, the present invention provides isolated host cells containing a nucleic acid construct or vector as broadly described above. In certain advantageous embodiments, the host cells are selected from bacterial cells, yeast cells and insect cells. [00621 In still another aspect, the present invention provides probes for interrogating 10 nucleic acid for the presence of a polynucleotide as broadly described above. These probes generally comprise a nucleotide sequence that hybridizes under at least low stringency conditions to a polynucleotide as broadly described above. In some embodiments, the probes consist essentially of a nucleic acid sequence which corresponds or is complementary to at least a portion of a nucleotide sequence encoding the amino acid sequence set forth in any one of 15 SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149,152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191,193,197, 199,201,203,205,207,209,211,213,215,217,219,221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249, wherein the portion is at least 15 20 nucleotides in length. In other embodiments, the probes comprise a nucleotide sequence which is capable of hybridizing to at least a portion of a nucleotide sequence encoding the amino acid sequence set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 25 159, 162,166,168, 172,174, 177,179, 181, 183, 189, 191, 193, 197, 199,201,203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249 under at least low stringency conditions, wherein the portion is at least 15 nucleotides in length. In still other embodiment, the probes comprise a nucleotide sequence that is capable of hybridizing to at least a portion of any one of SEQ ID NO: 1, 3, 4, 5, 7, 9, 11, 13, 15, 16, 17, 19, 21, 23, 24, 25, 30 26, 28, 29, 30, 32, 33, 34, 35, 37, 38, 39, 40, 41, 42, 44, 46, 48, 50, 51, 52, 54, 55, 56, 57, 59, 62, 63, 64, 66, 68, 70, 71, 73, 75, 77,'79, 81, 83, 85, 87, 89, 90, 91, 92, 93, 95, 96, 97, 99, 101, 103, 105, 107, 108, 109,111, 113, 115, 117, 118, 119, 121, 123, 125, 126, 127, 129, 130, 131, 133, 135, 137, 139, 141, 143, 144, 145, 147, 148, 150, 151, 153, 155, 156, 158, 160, 161, 163, 164, 165, 167, 169, 170, 171, 173, 175, 176, 178, 180, 182, 184, 185, 186, 187, 188, 190, 192, 35 194,195,196,198,200,202,204,206,208,210,212,214,216,218,220,222,224,226,228, 230, 232,233, 234, 236, 238, 239, 240, 241, 242, 243, 244, 246 or 248 under at least low stringency conditions, wherein the portion is at least 15 nucleotides in length. Representative -23 probes for detecting the stress marker polynucleotides according to the resent invention are set forth in SEQ ID NO: 250-1807 (see Table 2). 5 [00631 In a related aspect, the invention provides a solid or semi-solid support comprising at least one nucleic acid probe as broadly described above immobilized thereon. In some embodiments, the solid or semi-solid support comprises a spatial array of nucleic acid probes immobilized thereon. [00641 In a further aspect, the present invention provides isolated polypeptides, 10 referred to herein as "stress marker polypeptides," which are generally selected from: (i) a polypeptide comprising an amino acid sequence that shares at least 50% (and at least 51% to at least 99% and all integer percentages in between) sequence similarity with a polypeptide expression product of a stress marker gene as broadly described above, for example, especially a stress marker gene that comprises a nucleotide sequence that shares at least 50% (and at least 15 51% to at least 99% and all integer percentages in between) sequence identity with the sequence set forth in any one of SEQ ID NO: 15, 16, 23, 24, 25, 28, 29, 32, 33, 34, 37, 38, 39, 40, 41, 50, 51, 54, 55, 62, 63, 89, 90, 91, 92, 95, 96, 107, 108, 117, 118, 125, 126, 129, 130, 143, 144, 147, 150, 155, 163, 164, 169, 170, 175, 184, 185, 186, 187, 194, 195, 232, 233, 238, 239, 240, 241, 242 or 243; (ii) a portion of the polypeptide according to (i) wherein the portion comprises at 20 least 5 contiguous amino acid residues of that polypeptide; (iii) a polypeptide comprising an amino acid sequence that shares at least 30% similarity (and at least 31% to at least 99% and all integer percentages in between) with at least 15 contiguous amino acid residues of the polypeptide according to (i); and (iv) a polypeptide comprising an amino acid sequence that is immuno-interactive with an antigen-binding molecule that is immuno-interactive with a 25 sequence of (i), (ii) or (iii). 100651 Still a further aspect of the present invention provides an antigen-binding molecule that is immuno-interactive with a stress marker polypeptide as broadly described above. [00661 In a related aspect, the invention provides a solid or semi-solid support 30 comprising at least one antigen-binding molecule as broadly described above immobilized thereon. In some embodiments, the solid or semi-solid support comprises a spatial array of antigen-binding molecules immobilized thereon. -24 - [0067] Still another aspect of the invention provides the use of one or more stress marker polynucleotides as broadly described above, or the use of one or more probes as broadly described above, or the use of one or more stress marker polypeptides as broadly described 5 above, or the use of one or more antigen-binding molecules as broadly described above, in the manufacture of a kit for assessing the physiological response to stress or immune function in a subject. -25 - BRIEF DESCRIPTION OF THE DRAWINGS [00681 Figure 1 is a graphical representation of a receiver operating curve (ROC) for comparison of gene expression at 28 days after stressor to Day 0 (Day 0 is following 2 days of road transport). ROC curves are based on cross validated components discriminant function 5 scores. [0069] Figure 2 is a graphical representation of a receiver operating curve (ROC) for comparison of gene expression at 28 days after stressor to Day 2 (Day 0 is following 2 days of road transport). ROC curves are based on cross validated components discriminant function scores. 10 [0070] Figure 3 is a graphical representation of a receiver operating curve (ROC) for comparison of gene expression at 28 days after stressor to Day 4 (Day 0 is following 2 days of road transport). ROC curves are based on cross validated components discriminant function scores. [0071] Figure 4 is a graphical representation of a receiver operating curve (ROC) 15 for comparison of gene expression at 28 days after stressor to Day 7 (Day 0 is following 2 days of road transport). ROC curves are based on cross validated components discriminant function scores. [0072] Figure 5 is a graphical representation of a receiver operating curve (ROC) for comparison of gene expression at 28 days after stressor to Day 9 (Day 0 is following 2 days 20 of road transport). ROC curves are based on cross validated components discriminant function scores. [00731 Figure 6 is a graphical representation of a receiver operating curve (ROC) for comparison of gene expression at 28 days after stressor to Day 11 (Day 0 is following 2 days of road transport). ROC curves are based on cross validated components discriminant function 25 scores. [0074] Figure 7 is a graphical representation of a receiver operating curve (ROC) for comparison of gene expression at 28 days after stressor to Day 14 (Day 0 is following 2 days of road transport). ROC curves are based on cross validated components discriminant function scores. 30 [0075] Figure 8 is a graphical representation of a receiver operating curve (ROC) for comparison of gene expression at 28 days after stressor to Day 17 (Day 0 is following 2 days of road transport). ROC curves are based on cross validated components discriminant function scores. -26 - [00761 Figure 9 is a graphical representation of a receiver operating curve (ROC) for comparison of gene expression at 28 days after stressor to Day 21 (Day 0 is following 2 days of road transport). ROC curves are based on cross validated components discriminant function scores. 5 [00771 Figure 10 is a graphical representation of a receiver operating curve (ROC) for comparison of gene expression at 28 days after stressor to Day 24 (Day 0 is following 2 days of road transport). ROC curves are based on cross validated components discriminant function scores. -27 - DETAILED DESCRIPTION OF THE INVENTION 1. Definitions [00781 Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by those of ordinary skill in the art to which the 5 invention belongs. Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, preferred methods and materials are described. For the purposes of the present invention, the following terms are defined below. [00791 The articles "a" and "an" are used herein to refer to one or to more than one 10 (i.e. to at least one) of the grammatical object of the article. By way of example, "an element" means one element or more than one element. 100801 The term "aberrant expression," as used herein to describe the expression of a stress marker gene, refers to the overexpression or underexpression of a stress marker gene relative to the level of expression of the stress marker gene or variant thereof in cells obtained 15 from a healthy subject or from a subject free of stress, and/or to a higher or lower level of a stress marker gene product (e.g., transcript or polypeptide) in a tissue sample or body fluid obtained from a healthy subject or from a subject not under stress. In particular, a stress marker gene is aberrantly expressed if the level of expression of the stress marker gene is higher by at least about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80% or 90%, or even an at least about 20 100%, 200%, 300%, 400%, 500%, 600%, 700%, 800%, 900% or 1000%, or lower by at least about 10%, 20%, 30% 40%, 50%, 60%, 70%, 80%, 90%, 92%, 94%, 96%, 97%, 98% or 99%, or even an at least about 99.5%, 99.9%, 99.95%, 99.99%, 99.995% or 99.999% that the level of expression of the stress marker gene by cells obtained from a healthy subject or from a subject not under stress, and/or relative to the level of expression of the stress marker gene in a tissue 25 sample or body fluid obtained from a healthy subject or from a subject not under stress. [0081] By "about" is meant a quantity, level, value, number, frequency, percentage, dimension, size, amount, weight or length that varies by as much as 30, 25, 20, 25, 10, 9, 8, 7, 6, 5, 4, 3, 2 or I % to a reference quantity, level, value, number, frequency, percentage, dimension, size, amount, weight or length. 30 [0082] The term "amplicon" refers to a target sequence for amplification, and/or the amplification products of a target sequence for amplification. In certain other embodiments an "amplicon" may include the sequence of probes or primers used in amplification. [0083] By "antigen-binding molecule" is meant a molecule that has binding affinity for a target antigen. It will be understood that this term extends to immunoglobulins, -28immunoglobulin fragments and non-immunoglobulin derived protein frameworks that exhibit antigen-binding activity. [00841 As used herein, the term "binds specifically," "specifically immuno interactive" and the like when referring to an antigen-binding molecule refers to a binding 5 reaction which is determinative of the presence of an antigen in the presence of a heterogeneous population of proteins and other biologics. Thus, under designated immunoassay conditions, the specified antigen-binding molecules bind to a particular antigen and do not bind in a significant amount to other proteins or antigens present in the sample. Specific binding to an antigen under such conditions may require an antigen-binding molecule that is selected for its specificity for a 10 particular antigen. For example, antigen-binding molecules can be raised to a selected protein antigen, which bind to that antigen but not to other proteins present in a sample. A variety of immunoassay formats may be used to select antigen-binding molecules specifically immuno interactive with a particular protein. For example, solid-phase ELISA immunoassays are routinely used to select monoclonal antibodies specifically immuno-interactive with a protein. 15 See Harlow and Lane (1988) "Antibodies, A Laboratory Manual," Cold Spring Harbor Publications, New York, for a description of immunoassay formats and conditions that can be used to determine specific immunoreactivity. [0085] By "biologically active portion" is meant a portion of a full-length parent peptide or polypeptide which portion retains an activity of the parent molecule. As used herein, 20 the term "biologically active portion" includes deletion mutants and peptides, for example of at least about 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 40, 50, 60, 70, 80, 90, 100, 120, 150, 300, 400, 500, 600, 700, 800, 900, 1000 contiguous amino acids, which comprise an activity of a parent molecule. Portions of this type may be obtained through the application of standard recombinant nucleic acid techniques or synthesized using conventional 25 liquid or solid phase synthesis techniques. For example, reference may be made to solution synthesis or solid phase synthesis as described, for example, in Chapter 9 entitled "Peptide Synthesis" by Atherton and Shephard which is included in a publication entitled "Synthetic Vaccines" edited by Nicholson and published by Blackwell Scientific Publications. Alternatively, peptides can be produced by digestion of a peptide or polypeptide of the 30 invention with proteinases such as endoLys-C, endoArg-C, endoGlu-C and staphylococcus V8 protease. The digested fragments can be purified by, for example, high performance liquid chromatographic (HPLC) techniques. Recombinant nucleic acid techniques can also be used to produce such portions. [00861 The term "biological sample" as used herein refers to a sample that may be 35 extracted, untreated, treated, diluted or concentrated from an animal. The biological sample may include a biological fluid such as whole blood, serum, plasma, saliva, urine, sweat, ascitic fluid, -29 peritoneal fluid, synovial fluid, amniotic fluid, cerebrospinal fluid, tissue biopsy, and the like. In certain embodiments, the biological sample is blood, especially peripheral blood. [00871 As used herein, the term "cis-acting sequence", "cis-acting element" or "cis regulatory region" or "regulatory region" or similar term shall be taken to mean any sequence of 5 nucleotides, which when positioned appropriately relative to an expressible genetic sequence, is capable of regulating, at least in part, the expression of the genetic sequence. Those skilled in the art will be aware that a cis-regulatory region may be capable of activating, silencing, enhancing, repressing or otherwise altering the level of expression and/or cell-type-specificity and/or developmental specificity of a gene sequence at the transcriptional or post-transcriptional 10 level. In certain embodiments of the present invention, the cis-acting sequence is an activator sequence that enhances or stimulates the expression of an expressible genetic sequence. [00881 Throughout this specification, unless the context requires otherwise, the words "comprise," "comprises" and "comprising" will be understood to imply the inclusion of a stated step or element or group of steps or elements but not the exclusion of any other step or 15 element or group of steps or elements. [0089] By "corresponds to" or "corresponding to" is meant a polynucleotide (a) having a nucleotide sequence that is substantially identical or complementary to all or a portion of a reference polynucleotide sequence or (b) encoding an amino acid sequence identical to an amino acid sequence in a peptide or protein. This phrase also includes within its scope a peptide 20 or polypeptide having an amino acid sequence that is substantially identical to a sequence of amino acids in a reference peptide or protein. [0090] By "effective amount", in the context of treating or preventing a condition, is meant the administration of that amount of active to an individual in need of such treatment or prophylaxis, either in a single dose or as part of a series, that is effective for the prevention of 25 incurring a symptom, holding in check such symptoms, and/or treating existing symptoms, of that condition. The effective amount will vary depending upon the health and physical condition of the individual to be treated, the taxonomic group of individual to be treated, the formulation of the composition, the assessment of the medical situation, and other relevant factors. It is expected that the amount will fall in a relatively broad range that can be determined through 30 routine trials. [00911 The terms "expression" or "gene expression" refer to either production of RNA message or translation of RNA message into proteins or polypeptides. Detection of either types of gene expression in use of any of the methods described herein are part of the invention. [00921 By "expression vector" is meant any autonomous genetic element capable of 35 directing the transcription of a polynucleotide contained within the vector and suitably the -30synthesis of a peptide or polypeptide encoded by the polynucleotide. Such expression vectors are known to practitioners in the art. [00931 The term "gene" as used herein refers to any and all discrete coding regions of the cell's genome, as well as associated non-coding and regulatory regions. The gene is also 5 intended to mean the open reading frame encoding specific polypeptides, introns, and adjacent 5' and 3' non-coding nucleotide sequences involved in the regulation of expression. In this regard, the gene may further comprise control signals such as promoters, enhancers, termination and/or polyadenylation signals that are naturally associated with a given gene, or heterologous control signals. The DNA sequences may be cDNA or genomic DNA or a fragment thereof. The 10 gene may be introduced into an appropriate vector for extrachromosomal maintenance or for integration into the host. [0094] By "high density polynucleotide arrays" and the like is meant those arrays that contain at least 400 different features per cm 2 . [00951 The phrase "high discrimination hybridization conditions" refers to 15 hybridization conditions in which single base mismatch may be determined. [00961 "Hybridization" is used herein to denote the pairing of complementary nucleotide sequences to produce a DNA-DNA hybrid or a DNA-RNA hybrid. Complementary base sequences are those sequences that are related by the base-pairing rules. In DNA, A pairs with T and C pairs with G. In RNA U pairs with A and C pairs with G. In this regard, the terms 20 "match" and "mismatch" as used herein refer to the hybridization potential of paired nucleotides in complementary nucleic acid strands. Matched nucleotides hybridize efficiently, such as the classical A-T and G-C base pair mentioned above. Mismatches are other combinations of nucleotides that do not hybridize efficiently. [00971 The phrase "hybridizing specifically to" and the like refer to the binding, 25 duplexing, or hybridizing of a molecule only to a particular nucleotide sequence under stringent conditions when that sequence is present in a complex mixture (e.g., total cellular) DNA or RNA. [00981 Reference herein to "immuno-interactive" includes reference to any interaction, reaction, or other form of association between molecules and in particular where 30 one of the molecules is, or mimics, a component of the immune system. 100991 "Immune function" or "immunoreactivity" refers to the ability of the immune system to respond to foreign antigen as measured by standard assays well known in the art. [0100] The term "immunosuppression" refers to a decrease in the overall 35 immunoreactivity of the immune system resulting from stress or the physiological response to -31

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stress. Suitably, the decrease is by at least 20-40%, or by at least 50-75%, or even by at least 80% relative to the immunoreactivity in the absence of stress. Additionally, the term immunosuppressionn" includes within its scope a delay in the occurrence of the immune response as compared to a subject not under stress. A delay in the occurrence of an immune 5 response can be a short delay, for example I hr-10 days, i.e., 1 hr, 2, 5 or 10 days. A delay in the occurrence of an immune response can also be a long delay, for example, 10 days-10 years (i.e., 30 days, 60 days, 90 days, 180 days, 1, 2, 5 or 10 years). "Immunosuppression" according to the invention can also mean a decrease in the intensity of an immune response, e.g., a reduced intensity such that it is 5-100%, 25-100% or 75 -100% less than the intensity of the immune 10 response of a subject not compromised by stress. [01011 By "isolated" is meant material that is substantially or essentially free from components that normally accompany it in its native state. For example, an "isolated polynucleotide", as used herein, refers to a polynucleotide, which has been purified from the sequences which flank it in a naturally-occurring state, e.g., a DNA fragment which has been 15 removed from the sequences that are normally adjacent to the fragment. Alternatively, an "isolated peptide" or an "isolated polypeptide" and the like, as used herein, refer to in vitro isolation and/or purification of a peptide or polypeptide molecule from its natural cellular environment, and from association with other components of the cell, i.e., it is not associated with in vivo substances. 20 [0102] By "marker gene" is meant a gene that imparts a distinct phenotype to cells expressing the marker gene and thus allows such transformed cells to be distinguished from cells that do not have the marker. A selectable marker gene confers a trait for which one can 'select' based on resistance to a selective agent (e.g., a herbicide, antibiotic, radiation, heat, or other treatment damaging to untransformed cells). A screenable marker gene (or reporter gene) 25 confers a trait that one can identify through observation or testing, i.e., by 'screening' (e.g. p glucuronidase, luciferase, or other enzyme activity not present in untransformed cells). [01031 As used herein, a "naturally-occurring" nucleic acid molecule refers to a RNA or DNA molecule having a nucleotide sequence that occurs in nature. For example a naturally-occurring nucleic acid molecule can encode a protein that occurs in nature. 30 [01041 By "obtained from" is meant that a sample such as, for example, a cell extract or nucleic acid or polypeptide extract is isolated from, or derived from, a particular source. For instance, the extract may be isolated directly from biological fluid or tissue of the subject. [0105] The term "oligonucleotide" as used herein refers to a polymer composed of a 35 multiplicity of nucleotide residues (deoxyribonucleotides or ribonucleotides, or related structural variants or synthetic analogues thereof, including nucleotides with modified or -32substituted sugar groups and the like) linked via phosphodiester bonds (or related structural variants or synthetic analogues thereof). Thus, while the term "oligonucleotide" typically refers to a nucleotide polymer in which the nucleotide residues and linkages between them are naturally-occurring, it will be understood that the term also includes within its scope various 5 analogues including, but not restricted to, peptide nucleic acids (PNAs), phosphorothioate, phosphorodithioate, phophoroselenoate, phosphorodiselenoate, phosphoroanilothioate, phosphoraniladate, phosphoroamidate, methyl phosphonates, 2-0-methyl ribonucleic acids, and the like. The exact size of the molecule can vary depending on the particular application. Oligonucleotides are a polynucleotide subset with 200 bases or fewer in length. Preferably, 10 oligonucleotides are 10 to 60 bases in length and most preferably 12, 13, 14, 15, 16, 17, 18, 19, or 20 to 40 bases in length. Oligonucleotides are usually single stranded, e.g., for probes; although oligonucleotides may be double stranded, e.g., for use in the construction of a variant nucleic acid sequence. Oligonucleotides of the invention can be either sense or antisense oligonucleotides. 15 [0106] The term "oligonucleotide array" refers to a substrate having oligonucleotide probes with different known sequences deposited at discrete known locations associated with its surface. For example, the substrate can be in the form of a two dimensional substrate as described in U.S. Patent No. 5,424,186. Such substrate may be used to synthesize two dimensional spatially addressed oligonucleotide (matrix) arrays. Alternatively, the substrate 20 may be characterized in that it forms a tubular array in which a two dimensional planar sheet is rolled into a three-dimensional tubular configuration. The substrate may also be in the form of a microsphere or bead connected to the surface of an optic fibre as, for example, disclosed by Chee et al. in WO 00/39587. Oligonucleotide arrays have at least two different features and a density of at least 400 features per cm 2 . In certain embodiments, the arrays can have a density of 25 about 500, at least one thousand, at least 10 thousand, at least 100 thousand, at least one million or at least 10 million features per cm 2 . For example, the substrate may be silicon or glass and can have the thickness of a glass microscope slide or a glass cover slip, or may be composed of other synthetic polymers. Substrates that are transparent to light are useful when the method of performing an assay on the substrate involves optical detection. The term also refers to a probe 30 array and the substrate to which it is attached that form part of a wafer. [0107] The term "operably connected" or "operably linked" as used herein means placing a structural gene under the regulatory control of a promoter, which then controls the transcription and optionally translation of the gene. In the construction of heterologous promoter/structural gene combinations, it is generally preferred to position the genetic sequence 35 or promoter at a distance from the gene transcription start site that is approximately the same as the distance between that genetic sequence or promoter and the gene it controls in its natural setting; i.e., the gene from which the genetic sequence or promoter is derived. As is known in -33the art, some variation in this distance can be accommodated without loss of function. Similarly, the preferred positioning of a regulatory sequence element with respect to a heterologous gene to be placed under its control is defined by the positioning of the element in its natural setting; i.e., the genes from which it is derived. 5 [0108] The term "polynucleotide" or "nucleic acid" as used herein designates mRNA, RNA, cRNA, cDNA or DNA. The term typically refers to polymeric form of nucleotides of at least 10 bases in length, either ribonucleotides or deoxynucleotides or a modified form of either type of nucleotide. The term includes single and double stranded forms of DNA. 10 [0109] The terms "polynucleotide variant" and "variant" refer to polynucleotides displaying substantial sequence identity with a reference polynucleotide sequence or polynucleotides that hybridize with a reference sequence under stringent conditions that are defined hereinafter. These terms also encompass polynucleotides in which one or more nucleotides have been added or deleted, or replaced with different nucleotides. In this regard, it 15 is well understood in the art that certain alterations inclusive of mutations, additions, deletions and substitutions can be made to a reference polynucleotide whereby the altered polynucleotide retains a biological function or activity of the reference polynucleotide. The terms "polynucleotide variant" and "variant" also include naturally-occurring allelic variants. [01101 "Polypeptide", "peptide" and "protein" are used interchangeably herein to 20 refer to a polymer of amino acid residues and to variants and synthetic analogues of the same. Thus, these terms apply to amino acid polymers in which one or more amino acid residues is a synthetic non-naturally-occurring amino acid, such as a chemical analogue of a corresponding naturally-occurring amino acid, as well as to naturally-occurring amino acid polymers. [0111] The term "polypeptide variant" refers to polypeptides which are 25 distinguished from a reference polypeptide by the addition, deletion or substitution of at least one amino acid residue. In certain embodiments, one or more amino acid residues of a reference polypeptide are replaced by different amino acids. It is well understood in the art that some amino acids may be changed to others with broadly similar properties without changing the nature of the activity of the polypeptide (conservative substitutions) as described hereinafter. 30 [0112] By "primer" is meant an oligonucleotide which, when paired with a strand of DNA, is capable of initiating the synthesis of a primer extension product in the presence of a suitable polymerizing agent. The primer is preferably single-stranded for maximum efficiency in amplification but can alternatively be double-stranded. A primer must be sufficiently long to prime the synthesis of extension products in the presence of the polymerization agent. The 35 length of the primer depends on many factors, including application, temperature to be employed, template reaction conditions, other reagents, and source of primers. For example, -34depending on the complexity of the target sequence, the primer may be at least about 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 50, 75, 100, 150, 200, 300, 400, 500, to one base shorter in length than the template sequence at the 3' end of the primer to allow extension of a nucleic acid chain, though the 5' end of the primer may 5 extend in length beyond the 3' end of the template sequence. In certain embodiments, primers can be large polynucleotides, such as from about 35 nucleotides to several kilobases or more. Primers can be selected to be "substantially complementary" to the sequence on the template to which it is designed to hybridise and serve as a site for the initiation of synthesis. By "substantially complementary", it is meant that the primer is sufficiently complementary to 10 hybridise with a target polynucleotide. Desirably, the primer contains no mismatches with the template to which it is designed to hybridise but this is not essential. For example, non complementary nucleotide residues can be attached to the 5' end of the primer, with the remainder of the primer sequence being complementary to the template. Alternatively, non complementary nucleotide residues or a stretch of non-complementary nucleotide residues can 15 be interspersed into a primer, provided that the primer sequence has sufficient complementarity with the sequence of the template to hybridise therewith and thereby form a template for synthesis of the extension product of the primer. [0113] "Probe" refers to a molecule that binds to a specific sequence or sub sequence or other moiety of another molecule. Unless otherwise indicated, the term "probe" 20 typically refers to a polynucleotide probe that binds to another polynucleotide, often called the "target polynucleotide", through complementary base pairing. Probes can bind target polynucleotides lacking complete sequence complementarity with the probe, depending on the stringency of the hybridization conditions. Probes can be labeled directly or indirectly and include primers within their scope. 25 [01141 The term "recombinant polynucleotide" as used herein refers to a polynucleotide formed in vitro by the manipulation of nucleic acid into a form not normally found in nature. For example, the recombinant polynucleotide may be in the form of an expression vector. Generally, such expression vectors include transcriptional and translational regulatory nucleic acid operably linked to the nucleotide sequence. 30 [01151 By "recombinant polypeptide" is meant a polypeptide made using recombinant techniques, i.e., through the expression of a recombinant or synthetic polynucleotide. [0116] By "regulatory element" or "regulatory sequence" is meant nucleic acid sequences (e.g., DNA) necessary for expression of an operably linked coding sequence in a 35 particular host cell. The regulatory sequences that are suitable for prokaryotic cells for example, include a promoter, and optionally a cis-acting sequence such as an operator sequence and a -35 ribosome binding site. Control sequences that are suitable for eukaryotic cells include promoters, polyadenylation signals, transcriptional enhancers, translational enhancers, leader or trailing sequences that modulate mRNA stability, as well as targeting sequences that target a product encoded by a transcribed polynucleotide to an intracellular compartment within a cell or 5 to the extracellular environment. [0117] The term "sequence identity" as used herein refers to the extent that sequences are identical on a nucleotide-by-nucleotide basis or an amino acid-by-amino acid basis over a window of comparison. Thus, a "percentage of sequence identity" is calculated by comparing two optimally aligned sequences over the window of comparison, determining the 10 number of positions at which the identical nucleic acid base (e.g., A, T, C, G, 1) or the identical amino acid residue (e.g., Ala, Pro, Ser, Thr, Gly, Val, Leu, Ile, Phe, Tyr, Trp, Lys, Arg, His, Asp, Glu, Asn, Gln, Cys and Met) occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison (i.e., the window size), and multiplying the result by 100 to yield the 15 percentage of sequence identity. For the purposes of the present invention, "sequence identity" will be understood to mean the "match percentage" calculated by the DNASIS computer program (Version 2.5 for windows; available from Hitachi Software engineering Co., Ltd., South San Francisco, California, USA) using standard defaults as used in the reference manual accompanying the software. 20 [0118] "Similarity" refers to the percentage number of amino acids that are identical or constitute conservative substitutions as defined in Table 3 inf-a. Similarity may be determined using sequence comparison programs such as GAP (Deveraux et al. 1984, Nucleic Acids Research 12, 387-395). In this way, sequences of a similar or substantially different length to those cited herein might be compared by insertion of gaps into the alignment, such 25 gaps being determined, for example, by the comparison algorithm used by GAP. [0119] Terms used to describe sequence relationships between two or more polynucleotides or polypeptides include "reference sequence," "comparison window," "sequence identity," "percentage of sequence identity" and "substantial identity". A "reference sequence" is at least 12 but frequently 15 to 18 and often at least 25 monomer units, inclusive of 30 nucleotides and amino acid residues, in length. Because two polynucleotides may each comprise (1) a sequence (i.e., only a portion of the complete polynucleotide sequence) that is similar between the two polynucleotides, and (2) a sequence that is divergent between the two polynucleotides, sequence comparisons between two (or more) polynucleotides are typically performed by comparing sequences of the two polynucleotides over a "comparison window" to 35 identify and compare local regions of sequence similarity. A "comparison window" refers to a conceptual segment of at least 6 contiguous positions, usually about 50 to about 100, more -36usually about 100 to about 150 in which a sequence is compared to a reference sequence of the same number of contiguous positions after the two sequences are optimally aligned. The comparison window may comprise additions or deletions (i.e., gaps) of about 20% or less as compared to the reference sequence (which does not comprise additions or deletions) for 5 optimal alignment of the two sequences. Optimal alignment of sequences for aligning a comparison window may be conducted by computerized implementations of algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package Release 7.0, Genetics Computer Group, 575 Science Drive Madison, WI, USA) or by inspection and the best alignment (i.e., resulting in the highest percentage homology over the comparison window) 10 generated by any of the various methods selected. Reference also may be made to the BLAST family of programs as for example disclosed by Altschul et al., 1997, Nucl. Acids Res. 25:3389. A detailed discussion of sequence analysis can be found in Unit 19.3 of Ausubel et al., "Current Protocols in Molecular Biology", John Wiley & Sons Inc, 1994-1998, Chapter 15. [0120] The terms "subject" or "individual" or "patient", used interchangeably 15 herein, refer to any subject, particularly a vertebrate subject, and even more particularly a mammalian subject, for whom therapy or prophylaxis is desired. Suitable vertebrate animals that fall within the scope of the invention include, but are not restricted to, primates, avians, livestock animals (e.g., sheep, cows, horses, donkeys, pigs), laboratory test animals (e.g., rabbits, mice, rats, guinea pigs, hamsters), companion animals (e.g., cats, dogs) and captive wild 20 animals (e.g., foxes, deer, dingoes). A preferred subject is an equine animal in need of treatment or prophylaxis for stress. However, it will be understood that the aforementioned terms do not imply that symptoms are present. [0121] The phrase "substantially similar affinities" refers herein to target sequences having similar strengths of detectable hybridization to their complementary or substantially 25 complementary oligonucleotide probes under a chosen set of stringent conditions. [01221 The term "template" as used herein refers to a nucleic acid that is used in the creation of a complementary nucleic acid strand to the "template" strand. The template may be either RNA and/or DNA, and the complementary strand may also be RNA and/or DNA. In certain embodiments, the complementary strand may comprise all or part of the complementary 30 sequence to the "template," and/or may include mutations so that it is not an exact, complementary strand to the "template". Strands that are not exactly complementary to the template strand may hybridise specifically to the template strand in detection assays described here, as well as other assays known in the art, and such complementary strands that can be used in detection assays are part of the invention. -37- [0123] The term "transformation" means alteration of the genotype of an organism, for example a bacterium, yeast, mammal, avian, reptile, fish or plant, by the introduction of a foreign or endogenous nucleic acid. [0124] By "vector" is meant a polynucleotide molecule, suitably a DNA molecule 5 derived, for example, from a plasmid, bacteriophage, yeast, virus, mammal, avian, reptile or fish into which a polynucleotide can be inserted or cloned. A vector preferably contains one or more unique restriction sites and can be capable of autonomous replication in a defined host cell including a target cell or tissue or a progenitor cell or tissue thereof, or be integrable with the genome of the defined host such that the cloned sequence is reproducible. Accordingly, the 10 vector can be an autonomously replicating vector, i.e., a vector that exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g., a linear or closed circular plasmid, an extrachromosomal element, a minichromosome, or an artificial chromosome. The vector can contain any means for assuring self-replication. Alternatively, the vector can be one which, when introduced into the host cell, is integrated into 15 the genome and replicated together with the chromosome(s) into which it has been integrated. A vector system can comprise a single vector or plasmid, two or more vectors or plasmids, which together contain the total DNA to be introduced into the genome of the host cell, or a transposon. The choice of the vector will typically depend on the compatibility of the vector with the host cell into which the vector is to be introduced. The vector can also include a 20 selection marker such as an antibiotic resistance gene that can be used for selection of suitable transformants. Examples of such resistance genes are known to those of skill in the art. [01251 The terms "wild-type" and "normal" are used interchangeably to refer to the phenotype that is characteristic of most of the members of the species occurring naturally and contrast for example with the phenotype of a mutant. 25 2. Abbreviations [01261 The following abbreviations are used throughout the application: nt =nucleotide nts =nucleotides aa =amino acid(s) kb =kilobase(s) or kilobase pair(s) kDa =kilodalton(s) d=day h =hour s =seconds -38- 3. Markers of stress and uses therefor [0127] The present invention concerns measuring the stress level or physiological response to stress in a subject of interest. Markers of stress, in the form of RNA molecules of specified sequences, or polypeptides expressed from these RNA molecules in cells, especially in 5 blood cells, and more especially in peripheral blood cells, of subjects subjected to stress or perceived to be under stressful conditions, are disclosed. These markers are indicators of stress and, when differentially expressed, are diagnostic for a physiological response to stress in tested subjects. Such markers provide considerable advantages over the prior art in this field. In certain advantageous embodiments where peripheral blood is used for the analysis, it is possible to 10 monitor the reaction to stress, and in addition, the drawing of a blood sample is minimally invasive and relatively inexpensive. The detection methods disclosed herein are thus suitable for widespread screening of subjects. [01281 It will be apparent that the nucleic acid sequences disclosed herein will find utility in a variety of applications in assessing the response to stress, as well as managing and 15 treating stress. Examples of such applications within the scope of the present disclosure include amplification of stress markers using specific primers, detection of stress markers by hybridisation with oligonucleotide probes, incorporation of isolated nucleic acids into vectors, expression of vector-incorporated nucleic acids as RNA and protein, and development of immunological reagents corresponding to marker encoded products. 20 [01291 The identified stress markers may in turn be used to design specific oligonucleotide probes and primers. Such probes and primers may be of any length that would specifically hybridize to the identified marker gene sequences and may be at least about 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24,25, 26, 27, 28,29, 30, 35, 40, 50, 75, 100, 150, 200, 300, 400, 500 nucleotides in length and in the case of probes, up to the full length of the 25 sequences of the marker genes identified herein. Probes may also include additional sequence at their 5' and/or 3' ends so that they extent beyond the target sequence with which they hybridize. [0130] When used in combination with nucleic acid amplification procedures, these probes and primers enable the rapid analysis of biological samples (e.g., peripheral blood samples) for detecting or quantifying marker gene transcripts. Such procedures include any 30 method or technique known in the art or described herein for duplicating or increasing the number of copies or amount of a target nucleic acid or its complement. [01311 The identified markers may also be used to identify and isolate full-length gene sequences, including regulatory elements for gene expression, from genomic DNA libraries, which are suitably but not exclusively of equine origin. The cDNA sequences 35 identified in the present disclosure may be used as hybridization probes to screen genomic DNA libraries by conventional techniques. Once partial genomic clones have been identified, full -39 length genes may be isolated by "chromosomal walking" (also called "overlap hybridization") using, for example, the method disclosed by Chinault & Carbon (1979, Gene 5: 111-126). Once a partial genomic clone has been isolated using a cDNA hybridization probe, non-repetitive segments at or near the ends of the partial genomic clone may be used as hybridization probes in 5 further genomic library screening, ultimately allowing isolation of entire gene sequences for the stress markers of interest. It will be recognized that full-length genes may be obtained using the partial cDNA sequences or short expressed sequence tags (ESTs) described in this disclosure using standard techniques as disclosed for example by Sambrook, et al. (MOLECULAR CLONING. A LABORATORY MANUAL (Cold Spring Harbor Press, 1989) and Ausubel et 10 al., (CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley & Sons, Inc. 1994). In addition, the disclosed sequences may be used to identify and isolate full-length cDNA sequences using standard techniques as disclosed, for example, in the above-referenced texts. Sequences identified and isolated by such means may be useful in the detection of the stress marker genes using the detection methods described herein, and are part of the invention. 15 [0132] One of ordinary skill in the art could select segments from the identified marker genes for use in determining susceptibility, the different detection, diagnostic, or prognostic methods, vector constructs, antigen-binding molecule production, kit, and/or any of the embodiments described herein as part of the present invention. Marker gene sequences that are desirable for use in the invention are those set fort in SEQ ID NO: 1, 3, 4, 5, 7, 9, 11, 13, 15, 20 16, 17, 19, 21, 23, 24,25, 26, 28, 29, 30, 32, 33, 34, 35, 37, 38, 39, 40, 41, 42, 44, 46, 48, 50, 51, 52, 54, 55, 56, 57, 59, 62, 63, 64, 66, 68, 70, 71, 73, 75, 77,79, 81, 83, 85, 87, 89, 90, 91, 92, 93, 95, 96, 97, 99, 101, 103, 105, 107, 108, 109, 111, 113, 115, 117, 118, 119, 121, 123, 125, 126, 127, 129, 130, 131, 133, 135, 137, 139, 141, 143, 144, 145, 147, 148, 150, 151, 153, 155, 156, 158, 160, 161, 163, 164, 165, 167, 169, 170, 171, 173, 175, 176, 178, 180, 182, 184, 25 185, 186, 187, 188, 190,192,194,195,196,198,200,202,204,206,208,210,212,214,216, 218, 220, 222, 224, 226, 228, 230, 232, 233, 234, 236, 238, 239, 240, 241, 242, 243, 244, 246 or 248 (see Table 1). 4. Nucleic acid molecules of the invention [01331 As described in the Examples and in Table 1, the present disclosure provides 30 134 markers of stress (i.e., 134 stress marker genes), identified by GeneChipTM analysis of blood obtained from normal horses and from horses subjected to stress. Of the 134 marker genes, 96 have ful-length or substantially full-length coding sequences and the remaining 38 have partial sequence information at one or both of their 5' and 3' ends. The identified stress marker genes include 38 previously uncharacterised equine genes. 35 [01341 In accordance with the present invention, the sequences of isolated nucleic acids disclosed herein find utility inter alia as hybridization probes or amplification primers. -40- These nucleic acids may be used, for example, in diagnostic evaluation of biological samples or employed to clone full-length cDNAs or genomic clones corresponding thereto. In certain embodiments, these probes and primers represent oligonucleotides, which are of sufficient length to provide specific hybridization to a RNA or DNA sample extracted from the biological 5 sample. The sequences typically will be about 10-20 nucleotides, but may be longer. Longer sequences, e.g., of about 30, 40, 50, 100, 500 and even up to full-length, are desirable for certain embodiments. [0135] Nucleic acid molecules having contiguous stretches of about 10, 15, 17, 20, 30, 40, 50, 60, 75 or 100 or 500 nucleotides of a sequence set forth in any one of SEQ ID NO: 1, 10 3, 4,5, 7,9,11, 13, 15, 16, 17,19, 21, 23,24,25,26,28,29,30,32, 33,34, 35, 37, 38,39, 40, 41, 42, 44,46, 48, 50, 51, 52, 54, 55, 56, 57, 59, 62, 63, 64, 66, 68, 70, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 90, 91, 92, 93, 95, 96, 97, 99, 101, 103, 105, 107, 108, 109, 111, 113, 1.15, 117, 118, 119, 121, 123, 125, 126, 127, 129, 130, 131, 133, 135, 137, 139, 141, 143, 144, 145, 147, 148, 150, 151, 153, 155, 156, 158, 160, 161, 163, 164, 165, 167, 169, 170, 171, 173, 175, 176, 15 178, 180, 182, 184, 185, 186, 187, 188, 190, 192, 194, 195, 196, 198, 200, 202, 204, 206, 208, 210, 212, 214, 216, 218, 220, 222, 224, 226, 228, 230, 232, 233, 234, 236, 238, 239, 240, 241, 242, 243, 244, 246 or 248 are contemplated. Molecules that are complementary to the above mentioned sequences and that bind to these sequences under high stringency conditions are also contemplated. These probes are useful in a variety of hybridization embodiments, such as 20 Southern and northern blotting. In some cases, it is contemplated that probes may be used that hybridize to multiple target sequences without compromising their ability to effectively measure a stress response. In general, it is contemplated that the hybridization probes described herein are useful both as reagents in solution hybridization, as in PCR, for detection of expression of corresponding genes, as well as in embodiments employing a solid phase. 25 [0136] Various probes and primers may be designed around the disclosed nucleotide sequences. For example, in certain embodiments, the sequences used to design probes and primers may include repetitive stretches of adenine nucleotides (poly-A tails) normally attached at the ends of the RNA for the identified marker genes. In other embodiments, probes and primers may be specifically designed to not include these or other 30 segments from the identified marker genes, as one of ordinary skilled in the art may deem certain segments more suitable for use in the detection methods disclosed. In any event, the choice of primer or probe sequences for a selected application is within the realm of the ordinary skilled practitioner. Illustrative probe sequences for detection of stress marker genes are presented in Table 2. 35 [0137] Primers may be provided in double-stranded or single-stranded form, although the single-stranded form is desirable. Probes, while perhaps capable of priming, are -41 designed to bind to a target DNA or RNA and need not be used in an amplification process. In certain embodiments, the probes or primers are labelled with radioactive species 32 p, 14 C, 35S, 3H, or other label), with a fluorophore (e.g., rhodamine, fluorescein) or with a chemillumiscent label (e.g., luciferase). 5 [0138] The present invention provides 96 substantially full-length cDNA sequences as well as 59 EST or partial cDNA sequences that are useful as markers of stress. It will be understood, however, that the present disclosure is not limited to these disclosed sequences and is intended particularly to encompass at least isolated nucleic acids that are hybridizable to nucleic acids comprising the disclosed sequences or that are variants of these nucleic acids. For 10 example, a nucleic acid of partial sequence may be used to identify a structurally-related gene or the full-length genomic or cDNA clone from which it is derived. Methods for generating cDNA and genomic libraries which may be used as a target for the above-described probes are known in the art (see, for example, Sambrook et al., 1989, supra and Ausubel et aL., 1994, supra). All such nucleic acids as well as the specific nucleic acid molecules disclosed herein are 15 collectively referred to as "stress marker polynucleotides." Additionally, the present invention includes within its scope isolated or purified expression products of stress marker polynucleotides (i.e., RNA transcripts and polypeptides). [0139] Accordingly, the present invention encompasses isolated or substantially purified nucleic acid or protein compositions. An "isolated" or "purified" nucleic acid molecule 20 or protein, or biologically active portion thereof, is substantially or essentially free from components that normally accompany or interact with the nucleic acid molecule or protein as found in its naturally occurring environment. Thus, an isolated or purified polynucleotide or polypeptide is substantially free of other cellular material, or culture medium when produced by recombinant techniques, or substantially free of chemical precursors or other chemicals when 25 chemically synthesized. Suitably, an "isolated" polynucleotide is free of sequences (especially protein encoding sequences) that naturally flank the polynucleotide (i.e., sequences located at the 5' and 3' ends of the polynucleotide) in the genomic DNA of the organism from which the polynucleotide was derived. For example, in various embodiments, an isolated stress marker polynucleotide can contain less than about 5 kb, 4 kb, 3 kb, 2 kb, 1 kb, 0.5 kb, or 0.1 kb of 30 nucleotide sequences that naturally flank the polynucleotide in genomic DNA of the cell from which the polynucleotide was derived. A polypeptide that is substantially free of cellular material includes preparations of protein having less than about 30%, 20%, 10%, 5%, (by dry weight) of contaminating protein. When the protein of the invention or biologically active portion thereof is recombinantly produced, culture medium suitably represents less than about 35 30%, 20%, 10%, or 5% (by dry weight) of chemical precursors or non-protein-of-interest chemicals. -42- [0140] The present invention also encompasses portions of the full-length or substantially full-length nucleotide sequences of the stress marker genes or their transcripts or DNA copies of these transcripts. Portions of a stress marker nucleotide sequence may encode polypeptide portions or segments that retain the biological activity of the native polypeptide. 5 Alternatively, portions of a stress marker nucleotide sequence that are useful as hybridization probes generally do not encode amino acid sequences retaining such biological activity. Thus, portions of a stress marker nucleotide sequence may range from at least about 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 40, 50, 60, 80, 90, 100 nucleotides, or almost up to the full-length nucleotide sequence encoding the stress marker polypeptides of the invention. 10 [0141] A portion of a stress marker nucleotide sequence that encodes a biologically active portion of a stress marker polypeptide of the invention may encode at least about 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 40, 50, 60, 70, 80, 90, 100, 120, 150, 300, 400, 500, 600, 700, 800, 900 or 1000, or even at least about 2000, 3000, 4000 or 5000 contiguous amino acid residues, or almost up to the total number of amino acids present in 15 a full-length stress marker polypeptide. Portions of a stress marker nucleotide sequence that are useful as hybridization probes or PCR primers generally need not encode a biologically active portion of a stress marker polypeptide. [01421 Thus, a portion of a stress marker nucleotide sequence may encode a biologically active portion of a stress marker polypeptide, or it may be a fragment that can be 20 used as a hybridization probe or PCR primer using standard methods known in the art. A biologically active portion of a stress marker polypeptide can be prepared by isolating a portion of one of the stress marker nucleotide sequences of the invention, expressing the encoded portion of the stress marker polypeptide (e.g., by recombinant expression in vitro), and assessing the activity of the encoded portion of the stress marker polypeptide. Nucleic acid 25 molecules that are portions of a stress marker nucleotide sequence comprise at least about 15, 16, 17, 18, 19, 20, 25, 30, 50, 75, 100, 150, 200, 250, 300, 350, 400, 450, 500, 550, 600, or 650 nucleotides, or almost up to the number of nucleotides present in a full-length stress marker nucleotide sequence. 10143] The invention also contemplates variants of the stress marker nucleotide 30 sequences. Nucleic acid variants can be naturally-occurring, such as allelic variants (same locus), homologues (different locus), and orthologues (different organism) or can be non naturally occurring. Naturally occurring variants such as these can be identified with the use of well known molecular biology techniques, as, for example, with polymerase chain reaction (PCR) and hybridization techniques as known in the art. Non-naturally occurring variants can be made 35 by mutagenesis techniques, including those applied to polynucleotides, cells, or organisms. The variants can contain nucleotide substitutions, deletions, inversions and insertions. Variation can -43 occur in either or both the coding and non-coding regions. The variations can produce both conservative and non-conservative amino acid substitutions (as compared in the encoded product). For nucleotide sequences, conservative variants include those sequences that, because of the degeneracy of the genetic code, encode the amino acid sequence of one of the stress marker 5 polypeptides of the invention. Variant nucleotide sequences also include synthetically derived nucleotide sequences, such as those generated, for example, by using site-directed mutagenesis but which still encode a stress marker polypeptide of the invention. Generally, variants of a particular nucleotide sequence of the invention will have at least about 30%, 40% 50%, 55%, 60%, 65%, 70%, generally at least about 75%, 80%, 85%, desirably about 90% to 95% or more, 10 and more suitably about 98% or more sequence identity to that particular nucleotide sequence as determined by sequence alignment programs described elsewhere herein using default parameters. [01441 The stress marker nucleotide sequences of the invention can be used to isolate corresponding sequences and alleles from other organisms, particularly other mammals, 15 especially other equine species. Methods are readily available in the art for the hybridization of nucleic acid sequences. Coding sequences from other organisms may be isolated according to well known techniques based on their sequence identity with the coding sequences set forth herein. In these techniques all or part of the known coding sequence is used as a probe which selectively hybridizes to other stress marker coding sequences present in a population of cloned 20 genomic DNA fragments or cDNA fragments (i.e., genomic or cDNA libraries) from a chosen organism. Accordingly, the present invention also contemplates polynucleotides that hybridize to the stress marker gene nucleotide sequences, or to their complements, under stringency conditions described below. As used herein, the term "hybridizes under low stringency, medium stringency, high stringency, or very high stringency conditions" describes conditions for 25 hybridization and washing. Guidance for performing hybridization reactions can be found in Ausubel et al., (1998, supra), Sections 6.3.1-6.3.6. Aqueous and non-aqueous methods are described in that reference and either can be used. Reference herein to low stringency conditions include and encompass from at least about 1% v/v to at least about 15% v/v formamide and from at least about 1 M to at least about 2 M salt for hybridization at 42* C, and at least about 1 30 M to at least about 2 M salt for washing at 42* C. Low stringency conditions also may include 1% Bovine Serum Albumin (BSA), 1 mM EDTA, 0.5 M NaHPO 4 (pH 7.2), 7% SDS for hybridization at 65* C, and (i) 2 x SSC, 0.1% SDS; or (ii) 0.5% BSA, 1 mM EDTA, 40 mM NaHPO4 (pH 7.2), 5% SDS for washing at room temperature. One embodiment of low stringency conditions includes hybridization in 6 x sodium chloride/sodium citrate (SSC) at 35 about 450 C, followed by two washes in 0.2 x SSC, 0.1% SDS at least at 50* C (the temperature of the washes can be increased to 55* C for low stringency conditions). Medium stringency -44 conditions include and encompass from at least about 16% v/v to at least about 30% v/v formamide and from at least about 0.5 M to at least about 0.9 M salt for hybridization at 420 C, and at least about 0.1 M to at least about 0.2 M salt for washing at 550 C. Medium stringency conditions also may include 1% Bovine Serum Albumin (BSA), 1 mM EDTA, 0.5 M NaHPO4 5 (pH 7.2), 7% SDS for hybridization at 650 C, and (i) 2 x SSC, 0.1% SDS; or (ii) 0.5% BSA, 1 mM EDTA, 40 mM NaHPO 4 (pH 7.2), 5% SDS for washing at 60-65* C. One embodiment of medium stringency conditions includes hybridizing in 6 x SSC at about 450 C, followed by one or more washes in 0.2 x SSC, 0.1% SDS at 600 C. High stringency conditions include and encompass from at least about 31% v/v to at least about 50% v/v formamide and from about 10 0.01 M to about 0.15 M salt for hybridization at 420 C, and about 0.01 M to about 0.02 M salt for washing at 55* C. High stringency conditions also may include 1% BSA, 1 mM EDTA, 0.5 M NaHPO4 (pH 7.2), 7% SDS for hybridization at 650 C, and (i) 0.2 x SSC, 0.1% SDS; or (ii) 0.5% BSA, 1 mM EDTA, 40 mM NaHPO 4 (pH 7.2), 1% SDS for washing at a temperature in excess of 65* C. One embodiment of high stringency conditions includes hybridizing in 6 x 15 SSC at about 45* C, followed by one or more washes in 0.2 x SSC, 0.1% SDS at 650 C. [01451 In certain embodiments, a stress marker polynucleotide of the invention hybridises to a disclosed nucleotide sequence under very high stringency conditions. One embodiment of very high stringency conditions includes hybridising in 0.5 M sodium phosphate, 7% SDS at 650 C, followed by one or more washes at 0.2 x SSC, 1% SDS at 65* C. 20 [0146] Other stringency conditions are well known in the art and a skilled person will recognize that various factors can be manipulated to optimize the specificity of the hybridization. Optimization of the stringency of the final washes can serve to ensure a high degree of hybridization. For detailed examples, see Ausubel et al., supra at pages 2.10.1 to 2.10.16 and Sambrook et al. (1989, supra) at sections 1.101 to 1.104. 25 [0147] While stringent washes are typically carried out at temperatures from about 42* C to 68* C, one skilled in the art will appreciate that other temperatures may be suitable for stringent conditions. Maximum hybridization rate typically occurs at about 20* C to 25* C below the Tm for formation of a DNA-DNA hybrid. It is well known in the art that the Tm is the melting temperature, or temperature at which two complementary polynucleotide sequences 30 dissociate. Methods for estimating Tm are well known in the art (see Ausubel et al., supra at page 2.10.8). In general, the Tm of a perfectly matched duplex of DNA may be predicted as an approximation by the formula: [01481 Tm = 81.5 + 16.6 (logj0 M) + 0.41 (%G+C) - 0.63 (% formamide) (600/length) -45 - [01491 wherein: M is the concentration of Na+, preferably in the range of 0.01 molar to 0.4 molar; %G+C is the sum of guanosine and cytosine bases as a percentage of the total number of bases, within the range between 30% and 75% G+C; % formamide is the percent formamide concentration by volume; length is the number of base pairs in the DNA 5 duplex. The Tm of a duplex DNA decreases by approximately 1* C with every increase of 1% in the number of randomly mismatched base pairs. Washing is generally carried out at Tm - 15* C for high stringency, or Tm - 30* C for moderate stringency. [01501 In one example of a hybridization procedure, a membrane (e.g., a nitrocellulose membrane or a nylon membrane) containing immobilized DNA is hybridized 10 overnight at 420 C in a hybridization buffer (50% deionised formamide, 5 x SSC, 5 x Denhardt's solution (0.1% ficoll, 0.1% polyvinylpyrollidone and 0.1% bovine serum albumin), 0.1% SDS and 200 mg/mL denatured salmon sperm DNA) containing labeled probe. The membrane is then subjected to two sequential medium stringency washes (i.e., 2 x SSC, 0.1% SDS for 15 min at 450 C, followed by 2 x SSC, 0.1% SDS for 15 min at 50* C), followed by 15 two sequential higher stringency washes (i.e., 0.2 x SSC, 0.1% SDS for 12 min at 55* C followed by 0.2 x SSC and 0.1%SDS solution for 12 min at 65-68* C. 5. Polypeptides of the invention [01511 The present invention also contemplates full-length polypeptides encoded by the stress marker genes of the invention as well as the biologically active portions of those 20 polypeptides, which are referred to collectively herein as "stress marker polypeptides". Biologically active portions of full-length stress marker polypeptides include portions with immuno-interactive activity of at least about 6, 8, 10, 12, 14, 16, 18, 20, 25, 30, 40, 50, 60 amino acid residues in length. For example, immuno-interactive fragments contemplated by the present invention are at least 6 and desirably at least 8 amino acid residues in length, which can 25 elicit an immune response in an animal for the production of antigen-binding molecules that are immuno-interactive with a stress marker polypeptide of the invention. Such antigen-binding molecules can be used to screen other mammals, especially equine mammals, for structurally and/or functionally related stress marker polypeptides. Typically, portions of a full-length stress marker polypeptide may participate in an interaction, for example, an intramolecular or an inter 30 molecular interaction. An inter-molecular interaction can be a specific binding interaction or an enzymatic interaction (e.g., the interaction can be transient and a covalent bond is formed or broken). Biologically active portions of a full-length stress marker polypeptide include peptides comprising amino acid sequences sufficiently similar to or derived from the amino acid sequences of a (putative) full-length stress marker polypeptide, for example, the amino acid 35 sequences shown in SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, -46- 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249, which include less 5 amino acids than a full-length stress marker polypeptide, and exhibit at least one activity of that polypeptide. Typically, biologically active portions comprise a domain or motif with at least one activity of a full-length stress marker polypeptide. A biologically active portion of a full-length stress marker polypeptide can be a polypeptide which is, for example, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 40, 50, 60, 70, 80, 90, 100, 120, 150, 300, 10 400, 500, 600, 700, 800, 900 or 1000, or even at least about 2000, 3000, 4000 or 5000, or more amino acid residues in length. Suitably, the portion is a "biologically-active portion" having no less than about 1%, 10%, 25% 50% of the activity of the full-length polypeptide from which it is derived. [0152] The present invention also contemplates variant stress marker polypeptides. 15 "Variant" polypeptides include proteins derived from the native protein by deletion (so-called truncation) or addition of one or more amino acids to the N-terminal and/or C-terminal end of the native protein; deletion or addition of one or more amino acids at one or more sites in the native protein; or substitution of one or more amino acids at one or more sites in the native protein. Variant proteins encompassed by the present invention are biologically active, that is, 20 they continue to possess the desired biological activity of the native protein. Such variants may result from, for example, genetic polymorphism or from human manipulation. Biologically active variants of a native stress marker protein of the invention will have at least 40%, 50%, 60%, 70%, generally at least 75%, 80%, 85%, preferably about 90% to 95% or more, and more preferably about 98% or more sequence similarity with the amino acid sequence for the native 25 protein as determined by sequence alignment programs described elsewhere herein using default parameters. A biologically active variant of a protein of the invention may differ from that protein generally by as much 1000, 500, 400, 300, 200, 100, 50 or 20 amino acid residues or suitably by as few as 1-15 amino acid residues, as few as 1-10, such as 6-10, as few as 5, as few as 4, 3, 2, or even 1 amino acid residue. 30 [01531 A stress marker polypeptide of the invention may be altered in various ways including amino acid substitutions, deletions, truncations, and insertions. Methods for such manipulations are generally known in the art. For example, amino acid sequence variants of a stress marker protein can be prepared by -mutations in the DNA. Methods for mutagenesis and nucleotide sequence alterations are well known in the art. See, for example, Kunkel (1985, 35 Proc. NatL. Acad. Sci. USA 82:488-492), Kunkel et al. (1987, Methods in Enzymol. 154:367 382), U.S. Pat. No. 4,873,192, Watson, J. D. et al. ("Molecular Biology of the Gene", Fourth Edition, Benjamin/Cummings, Menlo Park, Calif., 1987) and the references cited therein. -47- Guidance as to appropriate amino acid substitutions that do not affect biological activity of the protein of interest may be found in the model of Dayhoff et al. (1978) Atlas of Protein Sequence and Structure (Nat]. Biomed. Res. Found., Washington, D.C.). Methods for screening gene products of combinatorial libraries made by point mutations or truncation, and for screening 5 cDNA libraries for gene products having a selected property are known in the art. Such methods are adaptable for rapid screening of the gene libraries generated by combinatorial mutagenesis of stress marker polypeptides. Recursive ensemble mutagenesis (REM), a technique which enhances the frequency of functional mutants in the libraries, can be used in combination with the screening assays to identify stress marker polypeptide variants (Arkin and Yourvan (1992) 10 Proc. NatI. Acad. Sci. USA 89:7811-7815; Delgrave et al. (1993) Protein Engineering 6:327 331). Conservative substitutions, such as exchanging one amino acid with another having similar properties, may be desirable as discussed in more detail below. [0154] Variant stress marker polypeptides may contain conservative amino acid substitutions at various locations along their sequence, as compared to the parent stress marker 15 amino acid sequence. A "conservative amino acid substitution" is one in which the amino acid residue is replaced with an amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined in the art, which can be generally sub-classified as follows: [0155] Acidic: The residue has a negative charge due to loss of H ion at 20 physiological pH and the residue is attracted by aqueous solution so as to seek the surface positions in the conformation of a peptide in which it is contained when the peptide is in aqueous medium at physiological pH. Amino acids having an acidic side chain include glutamic acid and aspartic acid. [01561 Basic: The residue has a positive charge due to association with H ion at 25 physiological pH or within one or two pH units thereof (e.g., histidine) and the residue is attracted by aqueous solution so as to seek the surface positions in the conformation of a peptide in which it is contained when the peptide is in aqueous medium at physiological pH. Amino acids having a basic side chain include arginine, lysine and histidine. 101571 Charged: The residues are charged at physiological pH and, therefore, 30 include amino acids having acidic or basic side chains (i.e., glutamic acid, aspartic acid, arginine, lysine and histidine). [0158] Hydrophobic: The residues are not charged at physiological pH and the residue is repelled by aqueous solution so as to seek the inner positions in the conformation of a peptide in which it is contained when the peptide is in aqueous medium. Amino acids having a 35 hydrophobic side chain include tyrosine, valine, isoleucine, leucine, methionine, phenylalanine and tryptophan. -48 - [01591 Neutral/polar: The residues are not charged at physiological pH, but the residue is not sufficiently repelled by aqueous solutions so that it would seek inner positions in the conformation of a peptide in which it is contained when the peptide is in aqueous medium. Amino acids having a neutral/polar side chain include asparagine, glutamine, cysteine, histidine, 5 serine and threonine. [01601 This description also characterizes certain amino acids as "small" since their side chains are not sufficiently large, even if polar groups are lacking, to confer hydrophobicity. With the exception of proline, "small" amino acids are those with four carbons or less when at least one polar group is on the side chain and three carbons or less when not. Amino acids 10 having a small side chain include glycine, serine, alanine and threonine. The gene-encoded secondary amino acid proline is a special case due to its known effects on the secondary conformation of peptide chains. The structure of proline differs from all the other naturally occurring amino acids in that its side chain is bonded to the nitrogen of the a-amino group, as well as the a-carbon. Several amino acid similarity matrices (e.g., PAM120 matrix and PAM250 15 matrix as disclosed for example by Dayhoff et al. (1978) A model of evolutionary change in proteins. Matrices for determining distance relationships In M. 0. Dayhoff, (ed.), Atlas of protein sequence and structure, Vol. 5, pp. 345-358, National Biomedical Research Foundation, Washington DC; and by Gonnet et al., 1992, Science 256(5062): 144301445), however, include proline in the same group as glycine, serine, alanine and threonine. Accordingly, for the 20 purposes of the present invention, proline is classified as a "small" amino acid. [01611 The degree of attraction or repulsion required for classification as polar or nonpolar is arbitrary and, therefore, amino acids specifically contemplated by the invention have been classified as one or the other. Most amino acids not specifically named can be classified on the basis of known behavior. 25 [0162] Amino acid residues can be further sub-classified as cyclic or noncyclic, and aromatic or nonaromatic, self-explanatory classifications with respect to the side-chain substituent groups of the residues, and as small or large. The residue is considered small if it contains a total of four carbon atoms or less, inclusive of the carboxyl carbon, provided an additional polar substituent is present; three or less if not. Small residues are, of course, always 30 nonaromatic. Dependent on their structural properties, amino acid residues may fall in two or more classes. For the naturally-occurring protein amino acids, sub-classification according to the this scheme is presented in the Table 3. [01631 Conservative amino acid substitution also includes groupings based on side chains. For example, a group of amino acids having aliphatic side chains is glycine, alanine, 35 valine, leucine, and isoleucine; a group of amino acids having aliphatic-hydroxyl side chains is serine and threonine; a group of amino acids having amide-containing side chains is asparagine -49and glutamine; a group of amino acids having aromatic side chains is phenylalanine, tyrosine, and tryptophan; a group of amino acids having basic side chains is lysine, arginine, and histidine; and a group of amino acids having sulfur-containing side chains is cysteine and methionine. For example, it is reasonable to expect that replacement of a leucine with an 5 isoleucine or valine, an aspartate with a glutamate, a threonine with a serine, or a similar replacement of an amino acid with a structurally related amino acid 'Will not have a major effect on the properties of the resulting variant polypeptide. Whether an amino acid change results in a functional stress marker polypeptide can readily be determined by assaying its activity. Conservative substitutions are shown in Table 4 under the heading of exemplary substitutions. 10 More preferred substitutions are shown under the heading of preferred substitutions. Amino acid substitutions falling within the scope of the invention, are, in general, accomplished by selecting substitutions that do not differ significantly in their effect on maintaining (a) the structure of the peptide backbone in the area of the substitution, (b) the charge or hydrophobicity of the molecule at the target site, or (c) the bulk of the side chain. After the substitutions are 15 introduced, the variants are screened for biological activity. [0164] Alternatively, similar amino acids for making conservative substitutions can be grouped into three categories based on the identity of the side chains. The first group includes glutamic acid, aspartic acid, arginine, lysine, histidine, which all have charged side chains; the second group includes glycine, serine, threonine, cysteine, tyrosine, glutamine, 20 asparagine; and the third group includes leucine, isoleucine, valine, alanine, proline, phenylalanine, tryptophan, methionine, as described in Zubay, G., Biochenisty, third edition, Wm.C. Brown Publishers (1993). [01651 Thus, a predicted non-essential amino acid residue in a stress marker polypeptide is typically replaced with another amino acid residue from the same side chain 25 family. Alternatively, mutations can be introduced randomly along all or part of a stress marker gene coding sequence, such as by saturation mutagenesis, and the resultant mutants can be screened for an activity of the parent polypeptide to identify mutants which retain that activity. Following mutagenesis of the coding sequences, the encoded peptide can be expressed recombinantly and the activity of the peptide can be determined. 30 [0166] Accordingly, the present invention also contemplates variants of the naturally-occurring stress marker polypeptide sequences or their biologically-active fragments, wherein the variants are distinguished from the naturally-occurring sequence by the addition, deletion, or substitution of one or more amino acid residues. In general, variants will display at least about 30, 40, 50, 55, 60, 65, 70, 75, 80, 85, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 % 35 similarity to a parent stress marker polypeptide sequence as, for example, set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20,22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, -50- 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112,114, 116,120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249. Desirably, variants will have at least 30, 40, 5 50, 55, 60, 65, 70, 75, 80, 85, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 % sequence identity to a parent stress marker polypeptide sequence as, for example, set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 10 183, 189, 191,193,197, 199,201,203,205,207,209,211,213,215,217,219,221,223,225, 227, 229, 231, 235, 237, 245, 247 or 249. Moreover, sequences differing from the native or parent sequences by the addition, deletion, or substitution of 1, 2, 3, 4, 5, 6, 7, 8,9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 30, 40, 50, 60 ,70, 80 ,90, 100, 150, 200, 300, 500 or more amino acids but which retain the properties of the parent stress marker polypeptide are contemplated. 15 stress marker polypeptides also include polypeptides that are encoded by polynucleotides that hybridise under stringency conditions as defined herein, especially high stringency conditions, to the stress marker polynucleotide sequences of the invention, or the non-coding strand thereof, as described above. [0167] In one embodiment, variant polypeptides differ from a stress marker 20 sequence by at least one but by less than 50, 40, 30, 20, 15, 10, 8, 6, 5, 4, 3 or 2 amino acid residue(s). In another, variant polypeptides differ from the corresponding sequence in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22,27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94,98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128,132,134,136,138, 140,142,146,149,152, 154, 157, 159, 162, 166, 168, 172, 174, 25 177, 179, 181, 183, 189, 191, 193, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249 by at least 1% but less than 20%, 15%, 10% or 5% of the residues. (If this comparison requires alignment the sequences should be aligned for maximum similarity. "Looped" out sequences from deletions or insertions, or mismatches, are considered differences.) The differences are, suitably, differences or changes at a 30 non-essential residue or a conservative substitution. 101681 A "non-essential" amino acid residue is a residue that can be altered from the wild-type sequence of an embodiment polypeptide without abolishing or substantially altering one or more of its activities. Suitably, the alteration does not substantially alter one of these activities, for example, the activity is at least 20%, 40%, 60%, 70% or 80% of wild-type. An 35 "essential" amino acid residue is a residue that, when altered from the wild-type sequence of a stress marker polypeptide of the invention, results in abolition of an activity of the parent molecule such that less than 20% of the wild-type activity is present. -51 - [0169] In other embodiments, a variant polypeptide includes an amino acid sequence having at least about 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94% 95%, 96%, 97%, 98% or more similarity to a corresponding sequence of a stress marker polypeptide as, for example, set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 5 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98,100,102,104,106,110,112,114,116, 120, 122,124,128, 132,134,136,138,140, 142, 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 197, 199,201,203,205,207, 209,211, 213,215,217,219,221,223,225,227,229,231, 235, 237, 245, 247 or 249, and has the activity of that stress marker polypeptide. 10 [0170] Stress marker polypeptides of the invention may be prepared by any suitable procedure known to those of skill in the art. For example, the polypeptides may be prepared by a procedure including the steps of: (a) preparing a chimeric cQnstruct comprising a nucleotide sequence that encodes at least a portion of a stress marker polynucleotide and that is operably linked to a regulatory element; (b) introducing the chimeric construct into a host cell; (c) 15 culturing the host cell to express the stress marker polypeptide; and (d) isolating the stress marker polypeptide from the host cell. In illustrative examples, the nucleotide sequence encodes at least a portion of the sequence set forth in any one of SEQ ID NO: 2, 6, 8, 10, 12, 14, 18, 20, 22, 27, 31, 36, 43, 45, 47, 49, 53, 58, 60, 61, 65, 67, 69, 72, 74, 76, 78, 80, 82, 84, 86, 88, 94, 98, 100, 102, 104, 106, 110, 112, 114, 116, 120, 122, 124, 128, 132, 134, 136, 138, 140, 142, 20 146, 149, 152, 154, 157, 159, 162, 166, 168, 172, 174, 177, 179, 181, 183, 189, 191, 193, 197, 199, 201, 203, 205, 207, 209, 211, 213, 215, 217, 219, 221, 223, 225, 227, 229, 231, 235, 237, 245, 247 or 249, or a variant thereof. [0171] The chimeric construct is typically in the form of an expression vector, which is suitably selected from self-replicating extra-chromosomal vectors (e.g., plasmids) and 25 vectors that integrate into a host genome. [01721 The regulatory element will generally be appropriate for the host cell employed for expression of the stress marker polynucleotide. Numerous types of expression vectors and regulatory elements are known in the art for a variety of host cells. Illustrative elements of this type include, but are not restricted to, promoter sequences (e.g., constitutive or 30 inducible promoters which may be naturally occurring or combine elements of more than one promoter), leader or signal sequences, ribosomal binding sites, transcriptional start and stop sequences, translational start and termination sequences, and enhancer or activator sequences. [0173] In some embodiments, the expression vector comprises a selectable marker gene to permit the selection of transformed host cells. Selectable marker genes are well known 35 in the art and will vary with the host cell employed. -52- [01741 The expression vector may also include a fusion partner (typically provided by the expression vector) so that the stress marker polypeptide is produced as a fusion polypeptide with the fusion partner. The main advantage of fusion partners is that they assist identification and/or purification of the fusion polypeptide. In order to produce the fusion 5 polypeptide, it is necessary to ligate the stress marker polynucleotide into an expression vector so that the translational reading frames of the fusion partner and the stress marker polynucleotide coincide. Well known examples of fusion partners include, but are not limited to, glutathione-S-transferase (GST), Fc potion of human IgG, maltose binding protein (MBP) and hexahistidine (HIS 6 ), which are particularly useful for isolation of the fusion polypeptide by 10 affinity chromatography. In some embodiments, fusion polypeptide5 are purified by affinity chromatography using matrices to which the fusion partners bind such as but not limited to glutathione-, amylose-, and nickel- or cobalt-conjugated resins. Many such matrices are available in "kit" form, such as the QIAexpressTM system (Qiagen) useful with (HIS 6 ) fusion partners and the Pharmacia GST purification system. Other fusion partners known in the art are 15 light-emitting proteins such as green fluorescent protein (GFP) and luciferase, which serve as fluorescent "tags" that permit the identification and/or isolation of fusion polypeptides by fluorescence microscopy or by flow cytometry. Flow cytometric methods such as fluorescence activated cell sorting (FACS) are particularly useful in this latter application. [01751 Desirably, the fusion partners also possess protease cleavage sites, such as 20 for Factor Xa or Thrombin, which permit the relevant protease to partially digest the fusion polypeptide and thereby liberate the stress marker polypeptide from the fusion construct. The liberated polypeptide can then be isolated from the fusion partner by subsequent chromatographic separation. [01761 Fusion partners also include within their scope "epitope tags," which are 25 usually short peptide sequences for which a specific antibody is available. Well known examples of epitope tags for which specific monoclonal antibodies are readily available include c-Myc, influenza virus, hemagglutinin and FLAG tags. [0177] The chimeric constructs of the invention are introduced into a host by any suitable means including "transduction" and "transfection," which are art recognized as 30 meaning the introduction of a nucleic acid, for example, an expression vector, into a recipient cell by nucleic acid-mediated gene transfer. "Transformation," however, refers to a process in which a host's genotype is changed as a result of the cellular uptake of exogenous DNA or RNA, and, for example, the transformed cell comprises the expression system of the invention. There are many methods for introducing chimeric constructs into cells. Typically, the method 35 employed will depend on the choice of host cell. Technology for introduction of chimeric constructs into host cells is well known to those of skill in the art. Four general classes of -53 methods for delivering nucleic acid molecules into cells have been described: (1) chemical methods such as calcium phosphate precipitation, polyethylene glycol (PEG)-mediate precipitation and lipofection; (2) physical methods such as microinjection, electroporation, acceleration methods and vacuum infiltration; (3) vector based methods such as bacterial and 5 viral vector-mediated transformation; and (4) receptor-mediated. Transformation techniques that fall within these and other classes are well known to workers in the art, and new techniques are continually becoming known. The particular choice of a transformation technology will be determined by its efficiency to transform certain host species as well as the experience and preference of the person practising the invention with a particular methodology of choice. It will 10 be apparent to the skilled person that the particular choice of a transformation system to introduce a chimeric construct into cells is not essential to or a limitation of the invention, provided it achieves an acceptable level of nucleic acid transfer. [0178] Recombinant stress marker polypeptides may be produced by culturing a host cell transformed with a chimeric construct. The conditions appropriate for expression of the 15 stress marker polynucleotide will vary with the choice of expression vector and the host cell and are easily ascertained by one skilled in the art through routine experimentation. Suitable host cells for expression may be prokaryotic or eukaryotic. An illustrative host cell for expression of a polypeptide of the invention is a bacterium. The bacterium used may be Escherichia coli. Alternatively, the host cell may be a yeast cell or an insect cell such as, for example, SF9 cells 20 that may be utilized with a baculovirus expression system. [0179] Recombinant stress marker polypeptides can be conveniently prepared using standard protocols as described for example in Sambrook, et al., (1989, supra), in particular Sections 16 and 17; Ausubel et al., (1994, supra), in particular Chapters 10 and 16; and Coligan et al., CURRENT PROTOCOLS IN PROTEIN SCIENCE (John Wiley & Sons, Inc. 1995 25 1997), in particular Chapters 1, 5 and 6. Alternatively, the stress marker polypeptides may be synthesized by chemical synthesis, e.g., using solution synthesis or solid phase synthesis as described, for example, in Chapter 9 of Atherton and Shephard (supra) and in Roberge et al (1995, Science 269: 202). 6. Antigen-binding molecules 30 101801 The invention also provides antigen-binding molecules that are specifically immuno-interactive with a stress marker polypeptide of the invention. In one embodiment, the antigen-binding molecule comprise whole polyclonal antibodies. Such antibodies may be prepared, for example, by injecting a stress marker polypeptide of the invention into a production species, which may include mice or rabbits, to obtain polyclonal antisera. Methods 35 of producing polyclonal antibodies are well known to those skilled in the art. Exemplary protocols which may be used are described for example in Coligan et al., CURRENT .54 - PROTOCOLS IN IMMUNOLOGY, (John Wiley & Sons, Inc, 1991), and Ausubel et al., (1994 1998, supra), in particular Section III of Chapter 11. [01811 In lieu of polyclonal antisera obtained in a production species, monoclonal antibodies may be produced using the standard method as described, for example, by Kbhler 5 and Milstein (1975, Nature 256, 495-497), or by more recent modifications thereof as described, for example, in Coligan et al., (1991, supra) by immortalizing spleen or other antibody producing cells derived from a production species which has been inoculated with one or more of the stress marker polypeptides of the invention. [0182] The invention also contemplates as antigen-binding molecules Fv, Fab, Fab' 10 and F(ab') 2 immunoglobulin fragments. Alternatively, the antigen-binding molecule may comprise a synthetic stabilized Fv fragment. Exemplary fragments of this type include single chain Fv fragments (sFv, frequently termed scFv) in which a peptide linker is used to bridge the N terminus or C terminus of a VH domain with the C terminus or N-terminus, respectively, of a VL domain. ScFv lack all constant parts of whole antibodies and are not able to activate 15 complement. ScFvs may be prepared, for example, in accordance with methods outlined in Kreber et al (Kreber et al. 1997, J. Immunol. Methods; 201(1): 35-55). Alternatively, they may be prepared by methods described in U.S. Patent No 5,091,513, European Patent No 239,400 or the articles by Winter and Milstein (1991, Nature 349:293) and Pl6ckthun et al (1996, In Antibody engineering: A practical approach. 203-252). In another embodiment, the synthetic 20 stabilised Fv fragment comprises a disulphide stabilised Fv (dsFv) in which cysteine residues are introduced into the Va and VL domains such that in the fully folded Fv molecule the two residues will form a disulphide bond between them. Suitable methods of producing dsFv are described for example in (Glockscuther et al. Biochem. 29: 1363-1367; Reiter et al. 1994, J Biol. Chem. 269: 18327-18331; Reiter et al. 1994, Biochem. 33: 5451-5459; Reiter et al. 1994. 25 Cancer Res. 54: 2714-2718; Webber et al. 1995, Mol. Immunol. 32: 249-258). [01831 Phage display and combinatorial methods for generating anti-stress marker polypeptide antigen-binding molecules are known in the art (as described in, e.g., Ladner et al. U.S. Patent No. 5,223,409; Kang et al. International Publication No. WO 92/18619; Dower et al. International Publication No. WO 91/17271; Winter et al. International Publication WO 30 92/2079 1; Markland et al. International Publication No. WO 92/15679; Breitling et al. International Publication WO 93/01288; McCafferty et al. International Publication No. WO 92/01047; Garrard et al. International Publication No. WO 92/09690; Ladner et al. International Publication No. WO 90/02809; Fuchs et al. (1991) Bio/Technology 9:1370-1372; Hay et al. (1992) Hum Antibod Hybridomas 3:81-85; Huse et al. (1989) Science 246:1275-1281; Griffths 35 et al. (1993) EMBO J 12:725-734; Hawkins et al. (1992) JMol Biol 226:889-896; Clackson et al. (1991) Nature 352:624-628; Gram et al. (1992) PNAS 89:3576-3580; Garrad et al. (1991) -55 - BiolTechnology 2:1373-1377; Hoogenboom et al. (1991) Nuc Acid Res 19:4133-4137; and Barbas et al. (1991) PNAS 88:7978-7982). The antigen-binding molecules can be used to screen expression libraries for variant stress marker polypeptides. They can also be used to detect and/or isolate the stress marker polypeptides of the invention. Thus, the invention also 5 contemplates the use of antigen-binding molecules to isolate stress marker polypeptides using, for example, any suitable immunoaffinity based method including, but not limited to, immunochromatography and immunoprecipitation. A suitable method utilises solid phase adsorption in which anti- stress marker polypeptide antigen-binding molecules are attached to a suitable resin, the resin is contacted with a sample suspected of containing a stress marker 10 polypeptide, and the stress marker p9lypeptide, if any, is subsequently eluted from the resin. Illustrative resins include: Sepharose@ (Pharmacia), Poros@ resins (Roche Molecular Biochemicals, Indianapolis), Actigel SuperflowTm resins (Sterogene Bioseparations Inc., Carlsbad Calif.), and Dynabeads T m (Dynal Inc., Lake Success, N.Y.). [01841 The antigen-binding molecule can be coupled to a compound, e.g., a label 15 such as a radioactive nucleus, or imaging agent, e.g. a radioactive, enzymatic, or other, e.g., imaging agent, e.g., a NMR contrast agent. Labels which produce detectable radioactive emissions or fluorescence are preferred. An anti- stress marker polypeptide antigen-binding molecule (e.g., monoclonal antibody) can be used to detect stress marker polypeptides (e.g., in a cellular lysate or cell supernatant) in order to evaluate the abundance and pattern of expression 20 of the protein. In certain advantageous application in accordance with the present invention, such antigen-binding molecules can be used to monitor stress marker polypeptides levels in biological samples (including whole cells and fluids) for diagnosing the presence, absence, degree, of stress or risk of development of disease as a consequences of stress. Detection can be facilitated by coupling (i.e., physically linking) the antibody to a detectable substance (i.e., 25 antibody labeling). Examples of detectable substances include various enzymes, prosthetic groups, fluorescent materials, luminescent materials, bioluminescent materials, and radioactive materials. Examples of suitable enzymes include horseradish peroxidase, alkaline phosphatase, p-galactosidase, or acetylcholinesterase; examples of suitable prosthetic group complexes include streptavidin/biotin and avidin/biotin; examples of suitable fluorescent materials include 30 umbelliferone, fluorescein, fluorescein isothiocyanate, rhodamine, dichlorotriazinylamine fluorescein, dansyl chloride or phycoerythrin; an example of a luminescent material includes luminol; examples of bioluminescent materials include luciferase, luciferin, and aequorin, and examples of suitable radioactive material include 12S, 1311, 35 S or 3 H. The label may be selected from a group including a chromogen, a catalyst, an enzyme, a fluorophore, a chemiluminescent 35 molecule, a lanthanide ion such as Europium (Eu 34 ), a radioisotope and a direct visual label. In the case of a direct visual label, use may be made of a colloidal metallic or non-metallic particle, -56a dye particle, an enzyme or a substrate, an organic polymer, a latex particle, a liposome, or other vesicle containing a signal producing substance and the like. [0185] A large number of enzymes useful as labels is disclosed in United States Patent Specifications U.S. 4,366,241, U.S. 4,843,000, and U.S. 4,849,338. Enzyme labels useful 5 in the present invention include alkaline phosphatase, horseradish peroxidase, luciferase, p galactosidase, glucose oxidase, lysozyme, malate dehydrogenase and the like. The enzyme label may be used alone or in combination with a second enzyme in solution. 7. Methods of detecting aberrant stress marker gene expression or alleles [0186] The present invention is predicated in part on the discovery that horses 10 subjected to stress have aberrant expression of certain genes or certain alleles of genes, referred to herein as stress marker genes, as compared to horses not subjected to stress. It is proposed that aberrant expression of these genes or their homologues or orthologues will be found in other animals under stress. Accordingly, the present invention features a method for assessing stress or for diagnosing stress or a stress-related condition (stress sequelae) in a subject, which 15 is suitably a mammal, by detecting aberrant expression of a stress marker gene in a biological sample obtained from the subject. According to some embodiments, the related condition is characterized by elevated levels of corticosteroids or their modulators (e.g., corticotropin releasing factor). Illustrative examples of such related conditions include: physical stress such as athletic training and physical trauma; mood disorders such as depression, including major 20 depression, single episode depression, recurrent depression, child abuse induced depression, seasonal affective disorder, postpartum depression, dysthemia, bipolar disorders, and cyclothymia; anxiety disorders including panic, phobias, obsessive-compulsive disorder; post traumatic stress disorder; and sleep disorders induced by stress; inflammation; pain; chronic fatigue syndrome; stress-induced headache; cancer; human immunodeficiency virus (HIV) 25 infections; neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease and Huntington's disease; gastrointestinal diseases such as ulcers, irritable bowel syndrome, Crohn's disease, spastic colon, diarrhea, and post operative ileus, and colonic hypersensitivity associated by psychopathological disturbances or stress; eating disorders such as anorexia and bulimia nervosa; supranuclear palsy; amyotrophic lateral sclerosis; a decrease in immune 30 function or immunosuppression; hemorrhagic stress; stress-induced psychotic episodes; euthyroid sick syndrome; syndrome of inappropriate antidiarrhetic hormone (ADH); overeating or obesity; infertility; head traumas; spinal cord trauma; ischemic neuronal damage (e.g., cerebral ischemia such as cerebral hippocampal ischemia); excitotoxic neuronal damage; epilepsy; cardiovascular disorders including hypertension, tachycardia and congestive heart 35 failure; stroke; immune dysfunctions including stress-induced immune dysfunctions (e.g., stress induced fevers, porcine stress syndrome, bovine shipping fever, equine paroxysmal fibrillation, -57and dysfunctions induced by confinement in chickens, sheering stress in sheep or human-animal interaction related stress in dogs); restraint; behavioral (operant) conditioning; muscular spasms; urinary incontinence; senile dementia of the Alzheimer's type; multiinfarct dementia; amyotrophic lateral sclerosis; chemical dependencies and addictions (e.g., dependencies on 5 alcohol, cocaine, heroin, benzodiazepines, or other drugs); drug and alcohol withdrawal symptoms; osteoporosis; psychosocial dwarfism; hypoglycemia; hair loss; abnormal circadian rhythm; and disorders related to abnormal circadian rhythm such as time zone change syndrome, seasonal affective disorder, sleep deprivation, irregular sleep-wake pattern, delayed sleep phase syndrome, advanced sleep phase syndrome, non-24 hour sleep wake disorder, light 10 induced clock resetting, REM sleep disorder, hypersomnia, parasomnia, narcolepsy, nocturnal enuresis, restless legs syndrome, sleep apnea, dysthymia, and abnormal circadian rhythm associated with chronic administration and withdrawal of antidepressant agents. [01871 In order to make the assessment or the diagnosis, it will be desirable to qualitatively or quantitatively determine the levels of stress marker gene transcripts, or the 15 presence of levels of particular alleles of a stress marker gene, or the level or functional activity of stress marker polypeptides. In some embodiments, the presence, degree or stage of stress or risk of development of stress sequelae is diagnosed when a stress marker gene product is present at a detectably lower level in the biological sample as compared t9 the level at which that gene is present in a reference sample obtained from normal subjects or from subjects not under stress. 20 In other embodiments, the presence, degree or stage of stress or risk of development of stress sequelae is diagnosed when a stress marker gene product is present at a detectably higher level in the biological sample as compared to the level at which that gene is present in a reference sample obtained from normal subjects or from subjects free of stress. Generally, such diagnoses are made when the level or functional activity of a stress marker gene product in the biological 25 sample varies from the level or functional activity of a corresponding stress marker gene product in the reference sample by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 92%, 94%, 96%, 97%, 98% or 99%, or even by at least about 99.5%, 99.9%, 99.95%, 99.99%, 99.995% or 99.999%, or even by at least about 100%, 200%, 300%, 400%, 500%, 600%, 700%, 800%, 900% or 1000%. Illustrative increases or decreases in the expression level of 30 representative stress marker genes are shown in Table 6. [01881 The corresponding gene product is generally selected from the same gene product that is present in the biological sample, a gene product expressed from a variant gene (e.g., an homologous or orthologous gene) including an allelic variant, or a splice variant or protein product thereof. In some embodiments, the method comprises measuring the level or 35 functional activity of individual expression products of at least about 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 or 30 stress marker genes. -58- [0189] Generally, the biological sample contains blood, especially peripheral blood, or a fraction or extract thereof. Typically, the biological sample comprises blood cells such as mature, immature and developing leukocytes, including lymphocytes, polymorphonuclear leukocytes, neutrophils, monocytes, reticulocytes, basophils, coelomocytes, hemocytes, 5 eosinophils, megakaryocytes, macrophages, dendritic cells natural killer cells, or fraction of such cells (e.g., a nucleic acid or protein fraction). In specific embodiments, the biological sample comprises leukocytes including peripheral blood mononuclear cells (PBMC). 7.1 Nucleic acid-based diagnostics [01901 Nucleic acid used in polynucleotide-based assays can be isolated from cells 10 contained in the biological sample, according to standard methodologies (Sambrook, et al., 1989, supra; and Ausubel et al., 1994, supra). The nucleic acid is typically fractionated (e.g., poly A+ RNA) or whole cell RNA. Where RNA is used as the subject of detection, it may be desired to convert the RNA to a complementary DNA. In some embodiments, the nucleic acid is amplified by a template-dependent nucleic acid amplification technique. A number of template 15 dependent processes are available to amplify the stress marker sequences present in a given template sample. An exemplary nucleic acid amplification technique is the polymerase chain reaction (referred to as PCR) which is described in detail in U,.S. Pat. Nos. 4,683,195, 4,683,202 and 4,800,159, Ausubel et al. (supra), and in Innis et al., ("PCR Protocols", Academic Press, Inc., San Diego Calif., 1990). Briefly, in PCR, two primer sequences are prepared that are 20 complementary to regions on opposite complementary strands of the marker sequence. An excess of deoxynucleoside triphosphates are added to a reaction mixture along with a DNA polymerase, e.g., Taq polymerase. If a cognate stress marker sequence is present in a sample, the primers will bind to the marker and the polymerase will cause the primers to be extended along the marker sequence by adding on nucleotides. By raising and lowering the temperature 25 of the reaction mixture, the extended primers will dissociate from the marker to form reaction products, excess primers will bind to the marker and to the reaction products and the process is repeated. A reverse transcriptase PCR amplification procedure may be performed in order to quantify the amount of mRNA amplified. Methods of reverse transcribing RNA into cDNA are well known and described in Sambrook et al., 1989, supra. Alternative methods for reverse 30 transcription utilize thermostable, RNA-dependent DNA polymerases. These methods are described in WO 90/07641. Polymerase chain reaction methodologies are well known in the art. [01911 In certain advantageous embodiments, the template-dependent amplification involves the quantification of transcripts in real-time. For example, RNA or DNA may be quantified using the Real-Time PCR technique (Higuchi, 1992, et al., Biotechnology 10: 413 35 417). By determining the concentration of the amplified products of the target DNA in PCR reactions that have completed the same number of cycles and are in their linear ranges, it is -59possible to determine the relative concentrations of the specific target sequence in the original DNA mixture. If the DNA mixtures are cDNAs synthesized from RNAs isolated from different tissues or cells, the relative abundance of the specific mRNA from which the target sequence was derived can be determined for the respective tissues or cells. This direct proportionality 5 between the concentration of the PCR products and the relative mRNA abundance is only true in the linear range of the PCR reaction. The final concentration of the target DNA in the plateau portion of the curve is determined by the availability of reagents in the reaction mix and is independent of the original concentration of target DNA. [0192] Another method for amplification is the ligase chain reaction ("LCR"), 10 disclosed in EPO No. 320 308. In LCR, two complementary probe pairs are prepared, and in the presence of the target sequence, each pair will bind to opposite complementary strands of the target such that they abut. In the presence of a ligase, the two probe pairs will link to form a single unit. By temperature cycling, as in PCR, bound ligated units dissociate from the target and then serve as "target sequences" for ligation of excess probe pairs. U.S. Pat. No. 4,883,750 15 describes a method similar to LCR for binding probe pairs to a target sequence. [01931 QP Replicase, described in PCT Application No. PCT/US87/00880, may also be used. In this method, a replicative sequence of RNA that has a region complementary to that of a target is added to a sample in the presence of an RNA polymerase. The polymerase will copy the replicative sequence that can then be detected. 20 [0194] An isothermal amplification method, in which restriction endonucleases and ligases are used to achieve the amplification of target molecules that contain nucleotide 5'a-thio triphosphates in one strand of a restriction site may also be useful in the amplification of nucleic acids in the present invention, Walker et al., (1992, Proc. Natl. Acad. Sci. U.S.A 89: 392-396). [01951 Strand Displacement Amplification (SDA) is another method of carrying out 25 isothermal amplification of nucleic acids which involves multiple rounds of strand displacement and synthesis, i.e., nick translation. A similar method, called Repair Chain Reaction (RCR), involves annealing several probes throughout a region targeted for amplification, followed by a repair reaction in which only two of the four bases are present. The other two bases can be added as biotinylated derivatives for easy detection. A similar approach is used in SDA. Target 30 specific sequences can also be detected using a cyclic probe reaction (CPR). In CPR, a probe having 3' and 5' sequences of non-specific DNA and a middle sequence of specific RNA is hybridized to DNA that is present in a sample. Upon hybridization, the reaction is treated with RNase H, and the products of the probe identified as distinctive products that are released after digestion. The original template is annealed to another cycling probe and the reaction is 35 repeated. -60- [01961 Still another amplification method described in GB Application No. 2 202 328, and in PCT Application No. PCT/IJS89/01025, may be used. In the former application, "modified" primers are used in a PCR-like, template- and enzyme-dependent synthesis. The primers may be modified by labeling with a capture moiety (e.g., biotin) and/or a detector 5 moiety (e.g., enzyme). In the latter application, an excess of labeled probes are added to a sample. In the presence of the target sequence, the probe binds and is cleaved catalytically. After cleavage, the target sequence is released intact to be bound by excess probe. Cleavage of the labeled probe signals the presence of the target sequence. 10197] Other nucleic acid amplification procedures include transcription-based 10 amplification systems (TAS), including nucleic acid sequence based amplification (NASBA) and 3SR (Kwoh et al., 1989, PrQc. Natl. Acad. Sci. US.A., 86: 1173; Gingeras et al., PCT Application WO 88/10315). In NASBA, the nucleic acids can be prepared for amplification by standard phenol/chloroform extraction, heat denaturation of a clinical sample, treatment with lysis buffer and minispin columns for isolation of DNA and RNA or guanidinium chloride 15 extraction of RNA. These amplification techniques involve annealing a primer which has target specific sequences. Following polymerization, DNA/RNA hybrids are digested with RNase H while double stranded DNA molecules are heat denatured again. In either case the single stranded DNA is made fully double stranded by addition of second target specific primer, followed by polymerization. The double-stranded DNA molecules are then multiply transcribed 20 by an RNA polymerase such as T7 or SP6. In an isothermal cyclic reaction, the RNAs are reverse transcribed into single stranded DNA, which is then converted to double stranded DNA, and then transcribed once again with an RNA polymerase such as T7 or SP6. The resulting products, whether truncated or complete, indicate target specific sequences. [0198] Davey et al., EPO No. 329 822 disclose a nucleic acid amplification process 25 involving cyclically synthesizing single-stranded RNA ("ssRNA"), ssDNA, and double stranded DNA (dsDNA), which may be used in accordance with the present invention. The ssRNA is a template for a first primer oligonucleotide, which is elongated by reverse transcriptase (RNA-dependent DNA polymerase). The RNA is then removed from the resulting DNA:RNA duplex by the action of ribonuclease H (RNase H, an RNase specific for RNA in 30 duplex with either DNA or RNA). The resultant ssDNA is a template for a second primer, which also includes the sequences of an RNA polymerase promoter (exemplified by T7 RNA polymerase) 5' to its homology to the template. This primer is then extended by DNA polymerase (exemplified by the large "Kienow" fragment of E. coli DNA polymerase I), resulting in a double-stranded DNA ("dsDNA") molecule, having a sequence identical to that of 35 the original RNA between the primers and having additionally, at one end, a promoter sequence. This promoter sequence can be used by the appropriate RNA polymerase to make many RNA copies of the DNA. These copies can then re-enter the cycle leading to very swift amplification. -61 - With proper choice of enzymes, this amplification can be done isothermally without addition of enzymes at each cycle. Because of the cyclical nature of this process, the starting sequence can be chosen to be in the form of either DNA or RNA. [01991 Miller et al. in PCT Application WO 89/06700 disclose a nucleic acid 5 sequence amplification scheme based on the hybridization of a promoter/primer sequence to a target single-stranded DNA ("ssDNA") followed by transcription of many RNA copies of the sequence. This scheme is not cyclic, i.e., new templates are not produced from the resultant RNA transcripts. Other amplification methods include "RACE" and "one-sided PCR" (Frohman, M. A., In: "PCR Protocols: A Guide to Methods and Applications", Academic Press, 10 N.Y., 1990; Ohara et al., 1989, Proc. Natl Acad. Sci. US.A., 86: 5673-567). [02001 Methods based on ligation of two (or more) oligonucleotides in the presence of nucleic acid having the sequence of the resulting "di-oligonucleotide", thereby amplifying the di-oligonucleotide, may also be used for amplifying target nucleic acid sequences. Wu et al., (1989, Genomics 4: 560). 15 [0201] Depending on the format, the stress marker nucleic acid of interest is identified in the sample directly using a template-dependent amplification as described, for example, above, or with a second, known nucleic acid following amplification. Next, the identified product is detected. In certain applications, the detection may be performed by visual means (e.g., ethidium bromide staining of a gel). Alternatively, the detection may involve 20 indirect identification of the product via chemiluminescence, radioactive scintigraphy of radiolabel or fluorescent label or even via a system using electrical or thermal impulse signals (Affymax Technology; Bellus, 1994, JMacromol. Sci. Pure, Appl. Chem., A31(1): 1355-1376). [02021 In some embodiments, amplification products or "amplicons" are visualized in order to confirm amplification of the stress marker sequences. One typical visualization 25 method involves staining of a gel with ethidium bromide and visualization under UV light. Alternatively, if the amplification products are integrally labeled with radio- or fluorometrically labeled nucleotides, the amplification products can then be exposed to x-ray film or visualized under the appropriate stimulating spectra, following separation. In some embodiments, visualization is achieved indirectly. Following separation of amplification products, a labeled 30 nucleic acid probe is brought into contact with the amplified stress marker sequence. The probe is suitably conjugated to a chromophore but may be radiolabeled. Alternatively, the probe is conjugated to a binding partner, such as an antigen-binding molecule, or biotin, and the other member of the binding pair carries a detectable moiety or reporter molecule. The techniques involved are well known to those of skill in the art and can be found in many standard texts on 35 molecular protocols (e.g., see Sambrook et al., 1989, supra and Ausubel et al. 1994, supra). For -62 example, chromophore or radiolabel probes or primers identify the target during or following amplification. . [0203] In certain embodiments, target nucleic acids are quantified using blotting techniques, which are well known to those of skill in the art. Southern blotting involves the use 5 of DNA as a target, whereas Northern blotting invQlves the use of RNA as a target. Each provide different types of information, although cDNA blotting is analogous, in many aspects, to blotting or RNA species. Briefly, a probe is used to target a DNA or RNA species that has been immobilized on a suitable matrix, often a filter of nitrocellulose. The different species should be spatially separated to facilitate analysis. This often is accomplished by gel 10 electrophoresis of nucleic acid species followed by "blotting" on to the filter. Subsequently, the blotted target is incubated with a probe (usually labeled) under conditions that promote denaturation and rehybridisation. Because the probe is designed to base pair with the target, the probe will bind a portion of the target sequence under renaturing conditions. Unbound probe is then removed, and detection is accomplished as described above. 15 [02041 Following detection/quantification, one may compare the results seen in a given subject with a control reaction or a statistically significant reference group of normal subjects or of subjects free of stress. In this way, it is possible to correlate the amount of a stress marker nucleic acid detected with the progression or severity of the disease. [0205] Also contemplated are genotyping methods and allelic discrimination 20 methods and technologies such as those described by Kristensen et al. (Biotechniques 30(2): 318-322), including the use of single nucleotide polymorphism analysis, high performance liquid chromatography, TaqMan

TM

, liquid chromatography, and mass spectrometry. [02061 Also contemplated are biochip-based technologies such as those described by Hacia et al. (1996, Nature Genetics 14: 441-447) and Shoemaker et al. (1996, Nature 25 Genetics 14: 450-456). Briefly, these techniques involve quantitative methods for analyzing large numbers of genes rapidly and accurately. By tagging genes with oligonucleotides or using fixed probe arrays, one can employ biochip technology to segregate target molecules as high density arrays and screen these molecules on the basis of hybridization. See also Pease et al. (1994, Proc. Natl. Acad. Sci. US.A. 91: 5022-5026); Fodor et al. (1991, Science 251: 767-773). 30 Briefly, nucleic acid probes to stress marker polynucleotides are made and attached to biochips to be used in screening and diagnostic methods, as outlined herein. The nucleic acid probes attached to the biochip are designed to be substantially complementary to specific expressed stress marker nucleic acids, i.e., the target sequence (either the target sequence of the sample or to other probe sequences, for example in sandwich assays), such that hybridization of the target 35 sequence and the probes of the present invention occurs. This complementarity need not be perfect; there may be any number of base pair mismatches which will interfere with -63hybridization between the target sequence and the nucleic acid probes of the present invention. However, if the number of mismatches is so great that no hybridization can occur under even the least stringent of hybridization conditions, the sequence is not a complementary target sequence. In certain embodiments, more than one probe per sequence is used, with either 5 overlapping probes or probes to different sections of the target being used. That is, two, three, four or more probes, with three being desirable, are used to build in a redundancy for a particular target. The probes can be overlapping (i.e. have some sequence in common), or separate. [02071 As will be appreciated by those of ordinary skill in the art, nucleic acids can 10 be attached to or immobilized on a solid support in a wide variety of ways. By "immobilized" and grammatical equivalents herein is meant the association or binding between the nucleic acid probe and the solid support is sufficient to be stable under the conditions of binding, washing, analysis, and removal as outlined below. The binding can be covalent or non-covalent. By "non covalent binding" and grammatical equivalents herein is meant one or more of either 15 electrostatic, hydrophilic, and hydrophobic interactions. Included in non-covalent binding is the covalent attachment of a molecule, such as, streptavidin to the support and the non-covalent binding of the biotinylated probe to the streptavidin. By "covalent binding" and grammatical equivalents herein is meant that the two moieties, the solid support and the probe, are attached by at least one bond, including sigma bonds, pi bonds and coordination bonds. Covalent bonds 20 can be formed directly between the probe and the solid support or can be formed by a cross linker or by inclusion of a specific reactive group on either the solid support or the probe or both molecules. Immobilization may also involve a combination of covalent and non-covalent interactions. [0208] In general, the probes are attached to the biochip in a wide variety of ways, 25 as will be appreciated by those in the art. As described herein, the nucleic acids can either be synthesized first, with subsequent attachment to the biochip, or can be directly synthesized on the biochip. 102091 The biochip comprises a suitable solid or semi-solid substrate or solid support. By "substrate" or "solid support" is meant any material that can be modified to contain 30 discrete individual sites appropriate for the attachment or association of the nucleic acid probes and is amenable to at least one detection method. As will be appreciated by practitioners in the art, the number of possible substrates are very large, and include, but are not limited to, glass and modified or functionalized glass, plastics (including acrylics, polystyrene and copolymiers of styrene and other materials, polypropylene, polyethylene, polybutylene, polyurethanes, 35 TeflonTm, etc.), polysaccharides, nylon or nitrocellulose, resins, silica or silica-based materials -64 including silicon and modified silicon, carbon, metals, inorganic glasses, plastics, etc. In general, the substrates allow optical detection and do not appreciably fluorescese. [02101 Generally the substrate is planar, although as will be appreciated by those of skill in the art, other configurations of substrates may be used as well. For example, the probes 5 may be placed on the inside surface of a tube, for flow-through sample analysis to minimize sample volume. Similarly, the substrate may be flexible, such as a flexible foam, including closed cell foams made of particular plastics. [02111 In certain embodiments, oligonucleotides probes are synthesized on the substrate, as is known in the art. For example, photoactivation techniques utilizing 10 photopolymerisation compounds and techniques can be used. In an illustrative example, the nucleic acids are synthesized in situ, using well known photolithographic techniques, such as those described in WO 95/25116; WO 95/35505; U.S. Pat. Nos. 5,700,637 and 5,445,934; and references cited within; these methods of attachment form the basis of the Affymetrix GeneChip T M technology. 15 [0212] In an illustrative biochip analysis, oligonucleotide probes on the biochip are exposed to or contacted with a nucleic acid sample suspected of containing one or more stress polynucleotides under conditions favoring specific hybridization. Sample extracts of DNA or RNA, either single or double-stranded, may be prepared from fluid suspensions of biological materials, or by grinding biological materials, or following a cell lysis step which includes, but 20 is not limited to, lysis effected by treatment with SDS (or other detergents), osmotic shock, guanidiniun isothiocyanate and lysozyme. Suitable DNA, which may be used in the method of the invention, includes cDNA. Such I)NA may be prepared by any one of a number of commonly used protocols as for example described in Ausubel, et al., 1994, supra, and Sambrook, et al., et al., 1989, supra. 25 10213] Suitable RNA, which may be used in the method of the invention, includes messenger RNA, complementary RNA transcribed from DNA (cRNA) or genomic or subgenomic RNA. Such RNA may be prepared using standard protocols as for example described in the relevant sections of Ausubel, et al. 1994, supra and Sambrook, et al. 1989, supra). 30 [0214] cDNA may be fragmented, for example, by sonication or by treatment with restriction endonucleases. Suitably, cDNA is fragmented such that resultant DNA fragments are of a length greater than the length of the immobilized oligonucleotide probe(s) but small enough to allow rapid access thereto under suitable hybridization conditions. Alternatively, fragments of cDNA may be selected and amplified using a suitable nucleotide amplification technique, as 35 described for example above, involving appropriate random or specific primers. -65 - [0215] Usually the target stress marker polynucleotides are detectably labeled so that their hybridization to individual probes can be determined. The target polynucleotides are typically detectably labeled with a reporter molecule illustrative examples of which include chromogens, catalysts, enzymes, fluorochromes, chemiluminescent molecules, bioluminescent 5 molecules, lanthanide ions (e.g., Eu"), a radioisotope and a direct visual label. In the case of a direct visual label, use may be made of a colloidal metallic or non-metallic particle, a dye particle, an enzyme or a substrate, an organic polymer, a latex particle, a liposome, or other vesicle containing a signal producing substance and the like. Illustrative labels of this type include large colloids, for example, metal colloids such as those from gold, selenium, silver, tin 10 and titanium oxide. In some embodiments in which an enzyme is used as a direct visual label, biotinylated bases are incorporated into a target polynucleotide. Hybridization is detected by incubation with streptavidin-reporter molecules. [9216] Suitable fluorochromes include, but are not limited to, fluorescein isothiocyanate (FITC), tetramethyirhodamine isothiocyanate (TRITC), R-Phycoerythrin (RPE), 15 and Texas Red. Other exemplary fluorochromes include those discussed by Dower ei al. (International Publication WO 93/06121). Reference also may be made to the fluorochromes described in U.S. Patents 5,573,909 (Singer et al), 5,326,692 (Brinkley et al). Alternatively, reference may be made to the fluorochromes described in U.S. Patent Nos. 5,227,487, 5,274,113, 5,405,975, 5,433,896, 5,442,045, 5,451,663, 5,453,517, 5,459,276, 5,516,864, 20 5,648,270 and 5,723,218. Commercially available fluorescent labels include, for example, fluorescein phosphoramidites such as FluoreprimeTm (Pharmacia), FluorediteM (Mvillipore) and FAM (Applied Biosystems International) [0217] Radioactive reporter molecules include, for example, 3 2 P, which can be detected by an X-ray or phosphoimager techniques. 25 [02181 The hybrid-forming step can be performed under suitable conditions for hybridizing oligonucleotide probes to test nucleic acid including DNA or RNA. In this regard, reference may be made, for example, to NUCLEIC ACID HYBRIDIZATION, A PRACTICAL APPROACH (Homes and Higgins, eds.) (IRL press, Washington D.C., 1985). In general, whether hybridization takes place is influenced by the length of the oligonucleotide probe and 30 the polynucleotide sequence under test, the pH, the temperature, the concentration of mono- and divalent cations, the proportion of G and C nucleotides in the hybrid-forming region, the viscosity of the medium and the possible presence of denaturants. Such variables also influence the time required for hybridization. The preferred conditions will therefore depend upon the particular application. Such empirical conditions, however, can be routinely determined without 35 undue experimentation. -66 - [0219] In certain advantageous embodiments, high discrimination hybridization conditions are used. For example, reference may be made to Wallace et al. (1979, Nucl. Acids Res. 6: 3543) who describe conditions that differentiate the hybridization of 11 to 17 base long oligonucleotide probes that match perfectly and are completely homologous to a target sequence 5 as compared to similar oligonucleotide probes that contain a single internal base pair mismatch. Reference also may be made to Wood et al. (1985, Proc. Natl. Acid. Sci. U$A 82: 1585) who describe conditions for hybridization of 11 to 20 base long oligonucleotides using 3M tetramethyl ammonium chloride wherein the melting point of the hybrid depends only on the length of the oligonwcleotide probe, regardless of its GC content. In addition, Drmanac et al. 10 (supra) describe hybridization conditions that allow stringent hybridization of 6-10 nucleotide long oligomers, and similar conditions may be obtained most readily by using nucleotide analogues such as 'locked nucleic acids (Christensen et al., 2001 Biochem J354: 481-4). [0220] Generally, a hybridization reaction can be performed in the presence of a hybridization buffer that optionally includes a hybridization optimizing agent, such as an 15 isostabilising agent, a denaturing agent and/or a renaturation accelerant. Examples of isostabilising agents include, but are not restricted to, betaines and lower tetraalkyl ammonium salts. Denaturing agents are compositions that lower the melting temperature of double stranded nucleic acid molecules by interfering with hydrogen bonding between bases in a double stranded nucleic acid or the hydration of nucleic acid molecules. Denaturing agents include, but 20 are not restricted to, formamide, formaldehyde, dimethylsulfoxide, tetraethyl acetate, urea, guanidium isothiocyanate, glycerol and chaotropic salts. Hybridization accelerants include heterogeneous nuclear ribonucleoprotein (hnRP) Al and cationic detergents such as cetyltrimethylammonium bromide (CTAB) and dodecyl trimethylammonium bromide (DTAB), polylysine, spermine, spermidine, single stranded binding protein (SSB), phage T4 gene 32 25 protein and a mixture of ammonium acetate and ethanol. Hybridization buffers may include target polynucleotides at a concentration between about 0.005 nM and about 50 nM, preferably between about 0.5 nM and 5 nM, more preferably between about 1 nM and 2 nM. [0221] A hybridization mixture containing the target stress marker polynucleotides is placed in contact with the array of probes and incubated at a temperature and for a time 30 appropriate to permit hybridization between the target sequences in the target polynucleotides and any complementary probes. Contact can take place in any suitable container, for example, a dish or a cell designed to hold the solid support on which the probes are bound. Generally, incubation will be at temperatures normally used for hybridization of nucleic acids, for example, between about 20* C and about 75* C, example, about 25* C, about 300 C, about 35* C, about 35 400 C, about 45* C, about 50* C, about 55* C, about 60* C, or about 65* C. For probes longer than 14 nucleotides, 200 C to 500 C is desirable. For shorter probes, lower temperatures are -67preferred. A sample of target polynucleotides is incubated with the probes for a time sufficient to allow the desired level of hybridization between the target sequences in the target polynucleotides and any complementary probes. For example, the hybridization may be carried out at about 450 C +/-100 C in formamide for 1-2 days. 5 102221 After the hybrid-forming step, the probes are washed to remove any unbound nucleic acid with a hybridization buffer, which can typically comprise a hybridization optimising agent in the same range of concentrations as for the hybridization step. This washing step leaves only bound target polynucleotides. The probes are then examined to identify which probes have hybridized to a target polynucleotide. 10 [0223] The hybridization reactions are then detected to determine which of the probes has hybridized to a corresponding target sequence. Depending on the nature of the reporter molecule associated with a target polynucleotide, a signal may be instrumentally detected by irradiating a fluorescent label with light and detecting fluorescence in a fluorimeter; by providing for an enzyme system to produce a dye which could be detected using a 15 spectrophotometer; or detection of a dye particle or a colored colloidal metallic or non metallic particle using a reflectometer; in the case of using a radioactive label or chemiluminescent molecule employing a radiation counter or autoradiography. Accordingly, a detection means may be adapted to detect or scan light associated with the label which light may include fluorescent, luminescent, focussed beam or laser light. In such a case, a charge couple device 20 (CCD) or a photocell can be used to scan for emission of light from a probe:target polynucleotide hybrid from each location in the micro-array and record the data directly in a digital computer. In some cases, electronic detection of the signal may not be necessary. For example, with enzymatically generated colour spots associated with nucleic acid array format, visual examination of the array will allow interpretation of the pattern on the array. In the case 25 of a nucleic acid array, the detection means is suitably interfaced with pattern recognition software to convert the pattern of signals from the array into a plain language genetic profile. In certain embodiments, oligonucleotide probes specific for different stress marker gene products are in the form of a nucleic acid array and detection of a signal generated from a reporter molecule on the array is performed using a 'chip reader'. A detection system that can be used by 30 a 'chip reader' is described for example by Pirrung et al (U.S. Patent No. 5,143,854). The chip reader will typically also incorporate some signal processing to determine whether the signal at a particular array position or feature is a true positive or maybe a spurious signal. Exemplary chip readers are described for example by Fodor et al (U.S. Patent No., 5,925,525). Alternatively, when the array is made using a mixture of individually addressable kinds of 35 labeled microbeads, the reaction may be detected using flow cytometry. -68 - 7.2 Protein-based diagnostics [02241 Consistent with the present invention, the presence of an aberrant concentration of a stress marker protein is indicative of the presence, degree or stage of stress or risk of development of stress sequelae. Stress marker protein levels in biological samples can be 5 assayed using any suitable method known in the art. For example, when a stress marker protein is an enzyme, the protein can be quantified based upon its catalytic activity or based upon the number of molecules of the protein contained in a sample. Antibody-based techniques may be employed, such as, for example, immunohistological and immunohistochemical methods for measuring the level of a protein of interest in a tissue sample. For example, specific recognition 10 is provided by a primary antibody (polyclonal or monoclonal) and a secondary detection system is used to detect presence (or binding) of the primary antibody. Detectable labels can be conjugated to the secondary antibody, such as a fluorescent label, a radiolabel, or an enzyme (e.g., alkaline phosphatase, horseradish peroxidase) which produces a quantifiable, e.g., colored, product. In another suitable method, the primary antibody itself can be detectably labeled. As a 15 result, immunohistological labeling of a tissue section is provided. In some embodiments, a protein extract is produced from a biological sample (e.g., tissue, cells) for analysis. Such an extract (e.g., a detergent extract) can be subjected to western-blot or dot/slot assay of the level of the protein of interest, using routine immunoblotting methods (Jalkanen et al., 1985, J. Cell. Biol. 101: 976-985; Jalkanen et al., 1987, J. Cell. Biol. 105: 3087-3096). 20 102251 Other useful antibody-based methods include immunoassays, such as the enzyme-linked immunosorbent assay (ELISA) and the radioimmunoassay (RIA). For example, a protein-specific monoclonal antibody, can be used both as an immunoadsorbent and as an enzyme-labeled probe to detect and quantify a stress marker protein of interest. The amount of such protein present in a sample can be calculated by reference to the amount present in a 25 standard preparation using a linear regression computer algorithm (see Lacobilli et al., 1988, Breast Cancer Research and Treatment 11: 19-30). In other embodiments, two different monoclonal antibodies to the protein of interest can be employed, one as the immunoadsorbent and the other as an enzyme-labeled probe. [02261 Additionally, recent developments in the field of protein capture arrays 30 permit the simultaneous detection and/or quantification of a large number of proteins. For example, low-density protein arrays on filter membranes, such as the universal protein array system (Ge, 2000 Nucleic Acids Res. 28(2):e3) allow imaging of arrayed antigens using standard ELISA techniques and a scanning charge-coupled device (CCD) detector. Immuno sensor arrays have also been developed that enable the simultaneous detection of clinical 35 analytes. It is now possible using protein arrays, to profile protein expression in bodily fluids, -69such as in sera of healthy or diseased subjects, as well as in subjects pre- and post-drug treatment [02271 Protein capture arrays typically comprise a plurality of protein-capture agents each of which defines a spatially distinct feature of the array. The protein-capture agent 5 can be any molecule or complex of molecules which has the ability to bind a protein and immobilize it to the site of the protein-capture agent on the array. The protein-capture agent may be a protein whose natural function in a cell is to specifically bind another protein, such as an antibody or a receptor. Alternatively, the protein-capture agent may instead be a partially or wholly synthetic or recombinant protein which specifically binds a protein. Alternatively, the 10 protein-capture agent may be a protein which has been selected in vitro from a mutagenized, randomized, or completely random and synthetic library by its binding affinity to a specific protein or peptide target. The selection method used may optionally have been a display method such as ribosome display or phage display, as known in the art. Alternatively, the protein capture agent obtained via in viiro selection may be a DNA or RNA aptamer which specifically 15 binds a protein target (see, e.g., Potyrailo et al., 1998 Anal. Chem. 70:3419-3425; Cohen et al., 1998, Proc. Natl. Acad. Sci. USA 95:14272-14277; Fukuda, et al., 1997 Nucleic Acids Symp. Ser. 37:237-238; available from SomaLogic). For example, aptamers are selected from libraries of oligonucleotides by the SelexTM process and their interaction with protein can be enhanced by covalent attachment, through incorporation of brominated deoxyuridine and UV-activated 20 crosslinking (photoaptamers). Aptamers have the advantages of ease of production by automated oligonucleotide synthesis and the stability and robustness of DNA; universal fluorescent protein stains can be used to detect binding. Alternatively, the in vitro selected protein-capture agent may be a polypeptide (e.g., an antigen) (see, e.g., Roberts and Szostak, 1997 Proc. Natl. Acad. Sci. USA, 94:12297-12302). 25 [02281 An alternative t9 an array of capture molecules is one made through 'molecular imprinting' technology, in which peptides (e.g., from the C-terminal regions of proteins) are used as templates to generate structurally complementary, sequence-specific cavities in a polymerizable matrix; the cavities can then specifically capture (denatured) proteins which have the appropriate primary amino acid sequence (e.g., available from ProteinPrintTM 30 and Aspira Biosystems). [0229] Exemplary protein capture arrays include arrays comprising spatially addressed antigen-binding molecules, commonly referred to as antibody arrays, which can facilitate extensive parallel analysis of numerous proteins defining a proteome or subproteome. Antibody arrays have been shown to have the required properties of specificity and acceptable 35 background, and some are available commercially (e.g., BD Biosciences, Clontech, BioRad and Sigma). Various methods for the preparation of antibody arrays have been reported (see, e.g., -70 - Lopez et al., 2003 J. Chromatogr. B 787:19-27; Cahill, 2000 Trends in Biotechnology 7:47-51; U.S. Pat. App. Pub. 2002/0055186; U.S. Pat. App. Pub. 2003/0003599; PCT publication WO 03/062444; PCT publication WO 03/077851; PCT publication WO 02/59601; PCT publication WO 02/39120; PCT publication WO 0 1/79849; PCT publication WO 99/39210). 5 The antigen-binding molecules of such arrays may recognize at least a subset of proteins expressed by a cell or population of cells, illustrative examples of which include growth factor receptors, hormone receptors, neurotransmitter receptors, catecholamine receptors, amino acid derivative receptors, cytokine receptors, extracellular matrix receptors, antibQdies, lectins, cytokines, serpins, proteases, kinases, phosphatases, ras-like GTPases, hydrolases, steroid 10 hormone receptors, transcription factors, heat-shock transcription factors, DNA-binding proteins, zinc-finger proteins, leucine-zipper proteins, homeodomain proteins, intracellular signal transduction modulators and effectors, apoptosis-related factors, DNA synthesis factors, DNA repair factors, DNA recombination factors, cell-surface antigens, hepatitis C virus (HCV) proteases and HIV proteases. 15 [0230] Antigen-binding molecules for antibody arrays are made either by conventional immunization (e.g., polyclonal sera and hybridomas), or as recombinant fragments, usually expressed in E coli, after selection from phage display or .ribosome display libraries (e.g., available from Cambridge Antibody Technology, BioInvent, Affitech and Biosite). Alternatively, 'combibodies' comprising non-covalent associations of VH and VL 20 domains, can be produced in a matrix format created from combinations of diabody-producing bacterial clones (e.g., available from Domantis). Exemplary antigen-binding molecules for use as protein-capture agents include monoclonal antibodies, polyclonal antibodies, Fv, Fab, Fab' and F(ab') 2 immunoglobulin fragments, synthetic stabilized Fv fragments, e.g., single chain Fv fragments (scFv), disulfide stabilized Fv fragments (dsFv), single variable region domains 25 (dAbs) minibodies, combibodies and multivalent antibodies such as diabodies and multi-scFv, single domains from camelids or engineered human equivalents. 10231] Individual spatially distinct protein-capture agents are typically attached to a support surface, which is generally planar or contoured. Common physical supports include glass slides, silicon, microwells, nitrocellulose or PVDF membranes, and magnetic and other 30 microbeads. [02321 While microdrops of protein delivered onto planar surfaces are widely used, related alternative architectures include CD centrifugation devices based on developments in microfluidics (e.g., available from Gyros) and specialized chip designs, such as engineered microchannels in a plate (e.g., The Living ChipTm, available from Biotrove) and tiny 3D posts 35 on a silicon surface (e.g., available from Zyomyx). -71 - [0233] Particles in suspension can also be used as the basis of arrays, providing they are coded for identification; systems include color-coding for microbeads (e.g., available from Luminex, Bio-Rad and Nanomics Biosystems) and semiconductor nanocrystals (e.g., QdotsTM, available from Quantum Dots), and barcoding for beads (UltraPlexTM, available from 5 Smartbeads) and multimetal microrods (NanobarcodesTM particles, available from Surromed). Beads can also be assembled into planar arrays on semiconductor chips (e.g., available from LEAPS technology and BioArray Solutions). Where particles are used, individual protein capture agents are typically attached to an individual particle to provide the spatial definition or separatiQn of the array. The particles may then be assayed separately, but in parallel, in a 10 compartmentalized way, for example in the wells of a microtiter plate or in separate test tubes. [0234] In operation, a protein sample, which is optionally fragmented to fQrm peptide fragments (see, e.g., U.S. Pat. App. Pub. 2002/0055186), is delivered to a protein capture array under conditions suitable for protein or peptide binding, and the array is washed to remove unbound or non-specifically bound components of the sample from the array. Next, the 15 presence or amount of protein or peptide bound to each feature of the array is detected using a suitable detection system. The amount of protein bound to a feature of the array may be determined relative to the amount of a second protein bound to a second feature of the array. In certain embodiments, the amount of the second protein in the sample is already known or known to be invariant. 20 [02351 For analyzing differential expression of proteins between two cells or cell populations, a protein sample of a first cell or population of cells is delivered to the array under conditions suitable for protein binding. In an analogous manner, a protein sample of a second cell or population of cells to a second array, is delivered to a second array which is identical to the first array. Both arrays are then washed to remove unbound or non-specifically bound 25 components of the sample from the arrays. In a final step, the amounts of protein remaining bound to the features of the first array are compared to the amounts of protein remaining bound to the corresponding features of the second array. To determine the differential protein expression pattern of the two cells or populations of cells, the amount of protein bound to individual features of the first array is subtracted from the amount of protein bound to the 30 corresponding features of the second array. [02361 In an illustrative example, fluorescence labeling can be used for detecting protein bound to the array. The same instrumentation as used for reading DNA microarrays is applicable to protein-capture arrays. For differential display, capture arrays (e.g. antibody arrays) can be probed with fluorescently labeled proteins from two different cell states, in which 35 cell lysates are labeled with different fluorophores (e.g., Cy-3 and Cy-5) and mixed, such that the color acts as a readout for changes in target abundance. Fluorescent readout sensitivity can -72 be amplified 10-100 fold by tyramide signal amplification (TSA) (e.g., available from PerkinElmer Lifesciences). Planar waveguide technology (e.g., available from Zeptosens) enables ultrasensitive fluorescence detection, with the additional advantage of no washing procedures. High sensitivity can also be achieved with suspension beads and particles, using 5 phycoerythrin as label (e.g., available from Luminex) or the properties of semiconductor nanocrystals (e.g., available from Quantum Dot). Fluorescence resonance energy transfer has been adapted to detect binding of unlabelled ligands, which may be useful on arrays (e.g., available from Affibody). Several alternative readouts have been developed, including adaptations of surface plasmon resonance (e.g., available from HTS Biosystems and Intrinsic 10 Bioprobes), rolling circle DNA amplification (e.g., available from Molecular Staging), mass spectrometry (e.g., available from Sense Proteomic, Ciphergen, Intrinsic and Bioprobes), resonance light scattering (e.g., available from Genicon Sciences) and atomic force microscopy (e.g., available from BioForce Laboratories). A microfluidics system for automated sample incubation with arrays on glass slides and washing has been co-developed by NextGen and 15 Perkin Elmer Life Sciences. [02371 In certain embodiments, the techniques used for detection of stress marker expression products will include internal or external standards to permit quantitative or semi quantitative determination of those products, to thereby enable a valid comparison of the level or functional activity of these expression products in a biological sample with the corresponding 20 expression products in a reference sample or samples. Such standards can be determined by the skilled practitioner using standard protocols. In specific examples, absolute values for the level or functional activity of individual expression products are determined. [0238] In specific embodiments, the diagnostic method is implemented using a system as disclosed, for example, in International Publication No. WO 02/090579 and in 25 copending PCT Application No. PCT/AU03/Q 1517 filed November 14, 2003, comprising at least one end station coupled to a base station. The base station is typically coupled to one or more databases comprising predetermined data from a number of individuals representing the level or functional activity of stress marker expression products, together with indications of the actual status of the individuals (e.g., presence, absence, degree, stage of stress or risk of 30 development of stress sequelae) when the predetermined data was collected. In operation, the base station is adapted to receive from the end station, typically via a communications network, subject data representing a measured or normalized level or functional activity of at least one expression product in a biological sample obtained from a test subject and to compare the subject data to the predetermined data stored in the database(s). Comparing the subject and 35 predetermined data allows the base station to determine the status of the subject in accordance with the results of the comparison. Thus, the base station attempts to identify individuals having -73 similar parameter values to the test subject and once the status has been determined on the basis of that identification, the base station provides an indication of the diagnosis to the end station. 7.3 Kits [0239] All the essential materials and reagents required for detecting and 5 quantifying stress marker gene expression products may be assembled together in a kit. The kits may also optionally include appropriate reagents for detection of labels, positive and negative controls, washing solutions, blotting membranes, microtiter plates dilution buffers and the like. For example, a nucleic acid-based detection kit may include (i) a stress marker polynucleotide (which may be used as a positive control), (ii) a primer or probe that specifically hybridizes to a 10 stress marker polynucleotide. Also included may be enzymes suitable for amplifying nucleic acids including various polymerases (Reverse Transcriptase, Taq, SequenaseTm DNA ligase etc. depending on the nucleic acid amplification technique employed), deoxynucleotides and buffers to provide the necessary reaction mixture for amplification. Such kits also generally will comprise, in suitable means, distinct containers for each individual reagent and enzyme as well 15 as for each primer or probe. Alternatively, a protein-based detection kit may include (i) a stress marker polypeptide (which may be used as a positive control), (ii) an antigen-binding molecule that is immuno-interactive with a stress marker polynucleotide. The kit can also feature various devices and reagents for performing one of the assays described herein; and/or printed instructions for using the kit to quantify the expression of a stress marker gene. 20 7.4 Monitoring immune function [0240] The present invention also provides methods for monitoring immune function by measuring the level or functional activity of an expression product of one or more stress marker genes in a subject. When the measured level or functional activity is the same as or similar to the measured level or functional activity of a corresponding expression product in a 25 reference sample obtained from one or more normal subjects or from one or more subjects not under stress, this generally indicates that the subject is not under stress and has normal immune function. Conversely, when the measured level or functional activity is different than the measured level or functional activity of the corresponding expression product, this generally indicates that the subject is under stress and consequently has reduced immune function (or 30 immunosuppression). [02411 The normalcy of immune function is important to the effective combat of disease and ultimate protection to natural challenge. In addition, it is vital to obtain an effective immune response to vaccination, and, in this regard, the identified stress markers can also be used to monitor the immune system of individuals so that vaccination can be timed to produce 35 an immune response that leads to the best level of protection. For instance, in the context of -74 athletic performance animals such as human athletes and racehorses, monitoring the immune system in this fashion allows the performance animal or his/her/its trainer to reduce potential stressors that may lead to an inappropriate or non-protective immune response to vaccination. When the performance animal's immune system has recovered, as determined by monitoring 5 using the identified stress markers, vaccination can be performed. [0242] Also, the identified stress markers can be used to assess the immune system's response to vaccine preparations. An inappropriate immune response to an initial vaccination may lead to a decision to revaccinate, or to modify the vaccination regimen, or to delay a vaccination regimen until potential stressors (that affect immune function) are removed 10 and the animal's immune system has recovered. [0243] By way of example, there are known vaccine preparations available for Equine Herpes Virus. It is widely used in the veterinary field, especially in pregnant mares so that foals will be afforded some protection through transfer of milk antibodies (colostrum). Pregnancy and the puerperal periods are times of high stress and immune modulation. Immune 15 function can be monitored during these periods using the identified stress markers, to time vaccination so that appropriate and protective vaccine responses are generated. Alternatively, stress marker levels could be used to modify the vaccination regimen depending upon the monitored immune response to vaccination. 8. Methods of treatment or prophylaxis 20 [0244] The present invention also extends to the treatment or prevention of stress in subjects following positive diagnosis for the risk of development of stress sequelae in the subjects. Generally, the treatment will include administering to a positively diagnosed subject an effective amount of an agent or therapy that ameliorates the symptoms or reverses the development of stress or that reduces or abrogates a stress-related condition as described for 25 example above, or that reduces potential of the subject to developing a stress-related condition. Current agents suitable for treating stress include, but are not limited to corticotropin-releasing factor antagonists as described, for example, in U.S. Patent Nos. 6,723,721, 6,670,371, 6,664,261, 6,586,456, 6,548,509, 6,323,312, 6,255,310; glucocorticoid receptor antagonists as disclosed in U.S. Patent Application Publication No. 20020169152; adenosine compounds as 30 described, for example, in U.S. Patent No. 6,642,209; nitric oxide donors as described, for example in U.S. Patent No. 6,455,542; nutritional compositions as described for example in U.S. Patent Nos. 6,444,700, 6,391,332 and 6,218,420; herbal extracts as disclosed, for example, in U.S. Patent No. 6,416,795; NK-l receptor antagonists as disclosed, for example, in U.S. Patent No. 6,087,348; fatty acid-based compositions as described, for example, in U.S. Patent 35 No. 6,077,867; peptide derivatives from yeast as disclosed, for example, in U.S. Patent -75 - Application Publication No. 20040101934; and zinc ionophores as described, for example, in U.S. Patent Application No. 20020183300; [02451 Alternatively, the subject may be treated using stress-relieving processes known in the art including for example: removing or decreasing the level of stressor in the 5 subject's environment; and altering ion flux across cell membranes with electric fields as described in U.S. Patent Application Publication No. 20030233124. [0246] However, it will be understood that the present invention encompasses any agent or process that is useful for treating or preventing stress and is not limited to the aforementioned illustrative compounds and formulations. 10 [02471 Typically, stress-relieving agents will be administered in pharmaceutical (or veterinary) compositions together with a pharmaceutically acceptable carrier and in an effective amount to achieve their intended purpose. The dose of active compounds administered to a subject should be sufficient to achieve a beneficial response in the subject over time such as a reduction in, or relief from, the symptoms of stress. The quantity of the pharmaceutically active 15 compounds(s) to be administered may depend on the subject to be treated inclusive of the age, sex, weight and general health condition thereof. In this regard, precise amounts of the active compound(s) for administration will depend on the judgement of the practitioner. In determining the effective amount of the active compound(s) to be administered in the treatment or prevention of stress, the physician or veterinarian may evaluate severity of any symptom 20 associated with the presence of stress including symptoms related to stress sequelae as mentioned above. In any event, those of skill in the art may readily determine suitable dosages of the stress relieving agents and suitable treatment regimens without undue experimentation. [02481 The stress relieving agents may be administered in concert with adjunctive therapies to reduce an aberrant immune response in the subject. Illustrative examples-of such 25 adjunctive therapies include but are not limited to, removal of the stressor, yoga, meditation, acupuncture, massage, mild exercise and breathing exercises. [0249] In order that the invention may be readily understood and put into practical effect, particular preferred embodiments will now be described by way of the following non limiting examples. -76- EXAMPLES EXAMPLE IDENTIFICATION OF SPECIFIC DIAGNOSTIC GENES FOR STRESS [02501 Blood samples obtained from 20 animals exposed to transport stress over 48 5 hours were analyzed using GeneChipsTm (method of use is described below in detail in "Generation of Gene Expression Data") containing thousands of genes expressed in white blood cells of horses. Analysis of these data (see "Identification of Responding Genes and Demonstration of Diagnostic Potential" below) reveals specific genes that are expressed differentially at day 0 through to day 28. It is possible to design an assay that measures the RNA 10 level in the sample using at least one and desirably at least two stress marker genes representative sequences of which are set forth in SEQ ID NO: 1, 3, 4, 5, 7, 9, 11, 13, 15, 16, 17, 19, 21, 23, 24, 25, 26, 28, 29, 30, 32, 33, 34, 35, 37, 38, 39, 40, 41, 42, 44, 46, 48, 50, 51, 52, 54, 55, 56, 57, 59, 62, 63, 64, 66, 68, 70, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 90, 91, 92, 93, 95, 96, 97, 99, 101, 103, 105, 107, 108, 109, 111, 113, 115, 117, 118, 119, 121, 123, 125, 15 126, 127, 129, 130, 131, 133, 135, 137, 139, 141, 143, 144, 145, 147, 148, 150, 151, 153, 155, 156, 158, 160, 161, 163, 164, 165, 167, 169, 170, 171, 173, 175, 176, 178, 180, 182, 184, 185, 186, 187, 188, 190, 192, 194, 195, 196, 198, 200, 202, 204, 206, 208, 210, 212, 214, 216, 218, 220, 222, 224, 226, 228, 230, 232, 233, 234, 236, 238, 239, 240, 241, 242, 243, 244, 246 or 248. Materials and Methods 20 Blood Collection [0251] BlQod is collected from a horse (in a non-agitated state) for the purpose of extraction of high quality RNA or protein. Suitable blood collection tubes for the collection, preservation, transport and isolation of RNA include PAXgeneTM tubes (PreAnalytix Inc., Valencia, CA, USA). Alternatively, blood can be collected into tubes containing solutions 25 designed for the preservation of nucleic acids (available from Roche, Ambion, Invitrogen and ABI). For the determination of protein levels, 50 mL of blood is prevented from clotting by collection into a tube containing 4 mL of 4% sodium citrate. White blood cells and plasma are isolated and stored frozen for later analysis and detection of specific proteins. PAXgene tubes can be kept at room temperature prior to RNA extraction. Clinical signs are recorded in a 30 standard format. Total RNA Extraction [0252] A kit available from Qiagen Inc (Valencia, CA, USA) has the reagents and instructions for the isolation of total RNA from 2.5 mL blood collected in the PAXgene Blood RNA Tube. Isolation begins with a centrifugation step to pellet nucleic acids in the PAXgene -77 blood RNA tube. The pellet is washed and resuspended and incubated in optimized buffers together with Proteinase K to bring about protein digestion. An additional centrifugation is carried out to remove residual cell debris and the supernatant is transferred to a fresh microcentrifuge tube. Ethanol is added to adjust binding conditions, and the lysate is applied to 5 the PAXgene RNA spin column. During brief centrifugation, RNA is selectively bound to the silica-gel membrane as contaminants pass through. Remaining contaminants are removed in three efficient wash steps and RNA is then eluted in Buffer BR5. [0253] Determination of RNA quantity and quality is necessary prior to proceeding and can be achieved using an Agilent Bioanalyzer and Absorbance 260/280 ratio using a 10 spectrophotometer. DNA Extraction [0254] A kit available from Qiagen Inc (Valencia, CA, USA) has the reagents and instructions for the isolation of total DNA from 8.5 mL blood collected in the PAXgene Blood DNA Tube. Isolation begins with the addition of additional lysis solution followed by a 15 centrifugation step. The pellet is washed and resuspended and incubated in optimized buffers together with Proteinase K to bring about protein digestion. DNA is precipitated using alcohol and an additional centrifugation is carried out to pellet the nucleic acid. Remaining contaminants are removed in a wash step and the DNA is then resuspended in Buffer BG4. [0255] Determination of DNA quantity and quality is necessary prior to proceeding 20 and can be achieved using a spectrophotometer or agarose gel electrophoresis. Generation of Gene Expression Data Choice of Method [02561 Measurement of specific RNA levels in a tissue sample can be achieved using a variety of technologies. Two common and readily available technologies that are well 25 known in the art are: [0257] GeneChip® analysis using Affymetrix technology. [02581 Real-Time Polymerase Chain Reaction (TaqManTM from Applied Biosystems for example). [02591 GeneChips® quantitate RNA by detection of labeled cRNA hybridized to 30 short oligonucleotides built on a silicon substrate. Details on the technology and methodology can be found at www.affymetrix.com. [02601 Real-Time Polymerase Chain Reaction (RT-PCR) quantitates RNA using two PCR primers, a labeled probe and a thermostable DNA polymerase. As PCR product is -78generated a dye is released into solution and detected. Internal controls such as 18S RNA probes are often used to determine starting levels of total RNA in the sample. Each gene and the internal control are run separately. Details on the technology and methods can be found at www.appliedbiosytems.com or www.qiagen.com or www.biorad..com. Applied Biosystems 5 offer a service whereby the customer provides DNA sequence information and payment and is supplied in return all of the reagents required to perform RT-PCR analysis on individual genes. [02611 GeneChip@ analysis has the advantage of being able to analyze thousands of genes at a time. However it is expensive and takes over 3 days to perform a single assay. RT PCR generally only analyses one gene at a time, but is inexpensive and can be completed within 10 a single day. [02621 RT-PCR is the method of choice for gene expression analysis if the number of specific genes to be analyzed is less than 20. GeneChip@ or other gene expression analysis technologies (such as Illumina Bead Arrays) are the method of choice when many genes need to be analysed simultaneously. 15 [0263] The methodology for GeneChip@ data generation and analysis and Real Time PCR is presented below in brief. GeneChip@ Data Generation cDNA & cRNA Generation: [02641 The following method for cDNA and cRNA generation from total RNA has 20 been adapted from the protocol provided and recommended by Affymetrix (www.affymetrix.com). [0265] The steps are: [02661 e A total of 3 pg of total RNA is used as a template to generate double stranded cDNA. 25 [02671 a cRNA is generated and labeled using biotinylated Uracil (dUTP). [0268] e biotin-labeled cRNA is cleaned and the quantity determined using a spectrophotometer and MOPS gel analysis. [02691 e labeled cRNA is fragmented to - 300bp in size. [02701 e RNA quantity is determined on an Agilent "Lab-on-a-Chip" system 30 (Agilent Technologies). -79 - Hybridization, Washing & Staining: [0271] The steps are: [02721 @ A hybridization cocktail is prepared containing 0.05 4pg/L of labeled and fragmented cRNA, spike-in positive hybridization controls, and the Affymetrix 5 oligonucleotides B2, bioB, bioC, bioD and cre. [0273] e The final volume (80 pL) of the hybridization cocktail is added to the GeneChip T m cartridge. [02741 e The cartridge is placed in a hybridization oven at constant rotation for 16 hours. 10 [02751 e The fluid is removed from the GeneChipTM and stored. [02761 e The GeneChipTM is placed in the fluidics station. [02771 * The experimental conditions for each GeneChipTM are recorded as an .EXP file. [0278] e All washing and staining procedures are carried out by the Affymetrix 15 fluidics station with an attendant providing the appropriate solutions. [02791 e The GeneChipTM is washed, stained with steptavidin-phycoerythin dye and then washed again using low salt solutions. [0280] * After the wash protocols are completed, the dye on the probe array is 'excited' by laser and the image captured by a CCD camera using an Affymetrix Scanner 20 (manufactured by Agilent). Scanning & Data File Generation: [02811 The scanner and MAS 5 software generates an image file from a single GeneChipTM called a .DAT file (see figure overleaf). [0282] The .DAT file is then pre-processed prior to any statistical analysis. 25 [0283] Data pre-processing steps (prior to any statistical analysis) include: [0284] e .DAT File Quality Control (QC). [0285] e .CEL File Generation. [0286] e Scaling and Normalization. -80 - .DAT File Quality Control [0287] The .DAT file is an image. The image is inspected manually for artifacts (e.g. high/low intensity spots, scratches, high regional or overall background). (The B2 oligonucleotide hybridization performance is easily identified by an alternating pattern of 5 intensities creating a border and array name.) The MAS 5 software used the B2 oligonucleotide border to align a grid over the image so that each square of oligonucleotides was centered and identified. [02881 The other spiked hybridization controls (bioB, bioC, bioD and cre) are used to evaluate sample hybridization efficiency by reading "present" gene detection calls with 10 increasing signal values, reflecting their relative concentrations. (If the .DAT file is of suitable quality it is converted to an intensity data file (.CEL file) by Affymetrix MAS 5 software). .CEL File Generation [0289] The .CEL files generated by the MAS 5 software from .DAT files contain calculated raw intensities for the probe sets. Gene expression data is obtained by subtracting a 15 calculated background from each cell value. To eliminate negative intensity values, a noise correction fraction based from a local noise value from the standard deviation of the lowest 2% of the background is applied. [0290] All .CEL files generated from the GeneChipTm are subjected to specific quality metrics parameters. 20 [02911 Some metrics are routinely recommended by Affymetrix and can be determined from Affymetrix internal controls provided as part of the GeneChipTM. Other metrics are based on experience and the processing of many GeneChipTM. Analysis of GeneChip@ Data [02921 Three illustrative approaches to normalizing data might be used: 25 [0293] Affymetrix MAS 5 Algorithm. [02941 e Robust Multi-chip Analysis (RMA) algorithm of Irizarry (Irizarray et al., 2002, Biostatistics (in print)). [0295] e Robust Multi-chip Analysis Saved model (RMAS). [0296] Those of skill in the art will recognize that many other approaches might be 30 adopted, without materially affecting the invention. -81 - Affymetrix MAS 5 Algorithm [0297] .CEL files are used by Affymetrix MAS 5 software to normalize or scale the data. Scaled data from one chip are compared to similarly scaled data from other chips. [0298] Affymetrix MAS 5 normalization is achieved by applying the default 5 "Global Scaling" option of the MAS 5 algorithm to the .CEL files. This procedure subtracts a robust estimate of the center of the distribution of probe values, and divides by a robust estimate of the probe variability. This produces a set of chips with common location and scale at the probe level. [0299] Gene expression indices are generated by a robust averaging procedure on 10 all the probe pairs for a given gene. The results are constrained to be non-negative. 10300] Given that scaling takes place at the level of the probe, rather than at the level of the gene, it is possible that even after normalization there may be chip-to-chip differences in overall gene expression level. Following standard MAS5 normalization, values for each gene were de-trended with respect to median chip intensity. That is, values for each 15 gene were regressed on the median chip intensity, and residuals were calculated. These residuals were taken as the de-trended estimates of expression for each gene [0301] Median chip intensity was calculated using the Affymetrix MASS algorithm, but with a scale factor fixed at one. RMAS Analysis 20 [03021 This method is identical to the RMA method, with the exception that probe weights and target quantiles are established using a long term library of chip .cel files, and are not re-calculated for these specific chips. Again, normalization occurs at the probe level. Real-Time PCR Data Generation [0303] Background information for conducting Real-time PCR may be obtained, for 25 example, at http://dorakmt.tripod.com/genetics/realtime.html and in a review by Bustin SA (2000, JMol Endocrinol 25:169-193). TaqManTM Primer and Probe Design Guidelines: [0304] 1. The Primer ExpressTM (ABI) software designs primers with a melting temperature (Tm) of 5 8-60* C, and probes with a Tm value of 10* C higher. The Tm of both 30 primers should be equal; [0305] 2. Primers should be 15-30 bases in length; -82- [03061 3. The G+C content should ideally be 30-80%. If a higher G+C content is unavoidable, the use of high annealing and melting temperatures, cosolvents such as glycerol, DMSO, or 7-deaza-dGTP may be necessary; [0307] 4. The run of an identical nucleotide should be avoided. This is especially 5 true for G, where runs of four or more Gs is not allowed; [0308] 5. The total number of Gs and Cs in the last five nucleotides at the 3' end of the primer should not exceed two (the newer version of the software has an option to do this automatically). This helps to introduce relative instability to the 3' end of primers to reduce non specific priming. The primer conditions are the same for SYBR Green assays; 10 [0309] 6. Maximum amplicon size should not exceed 400 bp (ideally 50-150 bases). Smaller amplicons give more consistent results because PCR is more efficient and more tolerant of reaction conditions (the short length requirement has nothing to do with the efficiency of 5' nuclease activity); [0310] 7. The probes should not have runs of identical nucleotides (especially four 15 or more consecutive Gs), G+C content should be 30-80%, there should be more Cs than Gs, and not a G at the 5' end. The higher number of Cs produces a higher ARn. The choice of probe should be made first; [0311] 8. To avoid false-positive results due to amplification of contaminating genomic DNA in the cDNA preparation, it is preferable to have primers spanning exon-exon 20 junctions. This way, genomic DNA will not be amplified (the PDAR kit for human GAPDH amplification has such primers); [0312] 9. If a TaqMan TM probe is designed for allelic discrimination, the mismatching nucleotide (the polymorphic site) should be in the middle of the probe rather than at the ends; 25 [0313] 10. Use primers that contain dA nucleotides near the 3' ends so that any primer-dimer generated is efficiently degraded by AmpErase T M UNG (mentioned in p.9 of the manual for EZ RT-PCR kit; P/N 402877). If primers cannot be selected with dA nucleotides near the ends, the use of primers with 3' terminal dU-nucleotides should be considered. [0314] (See also the general principles of PCR Primer Design by Invitrogen.) 30 General Method: [03151 1. Reverse transcription of total RNA to cDNA should be done with random hexamers (not with oligo-dT). If oligo-dT has to be used long mRNA transcripts or amplicons greater than two kilobases upstream should be avoided, and 18S RNA cannot be used as normaliser; -83 - [0316] 2. Multiplex PCR will only work properly if the control primers are limiting (ABI control reagents do not have their primers limited); [03171 3. The range of target cDNA used is 10 ng to I pg. If DNA is used (mainly for allelic discrimination studies), the optimum amount is 100 ng to 1 gg; 5 [03181 4. It is ideal to treat each RNA preparation with RNAse free DNAse to avoid genomic DNA contamination. Even the best RNA extraction methods yield some genomic DNA. Of course, it is ideal to have primers not amplifying genomic DNA at all but sometimes this may not be possible; [03191 5. For optimal results, the reagents (before the preparation of the PCR mix) 10 and the PCR mixture itself (before loading) should be vortexed and mixed well. Otherwise there may be shifting Rn value during the early (0 - 5) cycles of PCR. It is also important to add probe to the buffer component and allow it to equilibrate at room temperature prior to reagent mix formulation. TaqManTM Primers and Probes: 15 [03201 The TaqManTM probes ordered from ABI at midi-scale arrive already resuspended at 100 pM. If a 1/20 dilution is made, this gives a 5 pM solution. This stock solution should be aliquoted, frozen and kept in the dark. Using I L of this in a 50 L reaction gives the recommended 100 nM final concentration. [03211 The primers arrive lyophilized with the amount given on the tube in pmols 20 (such as 150.000 pmol which is equal to 150 nmol). If X nmol of primer is resuspended in X pL of H 2 0, the resulting solution is 1 mM. It is best to freeze this stock solution in aliquots. When the 1 mM stock solution is diluted 1/100, the resulting working solution will be 10 pM. To get the recommended 50 - 900 nM final primer concentration in 50 p.L reaction volume, 0.25 - 4.50 L should be used per reaction (2.5 p.L for 500 nM final concentration). 25 [03221 The PDAR primers and probes are supplied as a mix in one tube. They have to be used 2.5 pL in a 50 L reaction volume. Setting up One-step TaqManTM Reaction: [03231 One-step real-time PCR uses RNA (as opposed to cDNA) as a template. This is the preferred method if the RNA solution has a low concentration but only if singleplex 30 reactions are run. The disadvantage is that RNA carryover prevention enzyme AmpErase cannot be used in one-step reaction format. In this method, both reverse transcriptase and real-time PCR take place in the same tube. The downstream PCR primer also acts as the primer for reverse transcriptase (random hexamers or oligo-dT cannot be used for reverse transcription in -84 one-step RT-PCR). One-step reaction requires higher dNTP concentration (greater than or equal to 300 mM vs 200 mM) as it combines two reactions needing dNTPs in one. A typical reaction mix for one-step PCR by Gold RT-PCR kit is as follows: Reagns. Volume

H

2 0 + RNA: 20.5 RL [24 gL if PDAR is used] 1oX TaqMan buffer: 5.0 pL MgCl 2 (25 mM): 11.0 PL dATP (10mM): 1.5 pL [for final concentration of 300 pM] dCTP (10mM): 1.5 pL [for final concentration of 300 pM] dGTP (10mM): 1.5 pL [for final concentration of 300 pM] dUTP (20mM): 1.5 IL [for final concentration of 600 pM] Primer F (10 pM) *: 2.5 gL [for final concentration of 500 nM] Primer R (10 pM) *: 2.5 pL [for final concentration of 500 nM] TaqMan Probe *: 1.0 pL [for final concentration of 100 nM] AmpliTaq Gold: 0.25 pL [can be increased for higher efficiency] Reverse Transcriptase: 0.25 pL RNAse inhibitor: 1.00 pL [0324] If a PDAR is used, 2.5 4L of primer + probe mix used. 5 [03251 Ideally 10 pg - 100 ng RNA should be used in this reaction. Note that decreasing the amount of template from 100 ng to 50 ng will increase the Cr value by 1. To decrease a CT value by 3, the initial amount of template should be increased 8-fold. ABI claims that 2 picograms of RNA can be detected by this system and the maximum amount of RNA that can be used is 1 microgram. For routine analysis, 10 pg - 100 ng RNA and 100 pg - 1 pg 10 genomic DNA can be used. Cycling Parameters for One-step PCR: [0326] Reverse transcription (by MuLV) 48* C for 30 min. [03271 AmpliTaq activation 95* C for 10 min. [03281 PCR: denaturation 95* C for 15 sec and annealing/extension 60* C for I min 15 (repeated 40 times) (On ABI 7700, minimum holding time is 15 seconds.) [0329] The recently introduced EZ one-step" m RT-PCR kit allows the use of UNG as the incubation time for reverse transcription is 600 C thanks to the use of a thermostable -85reverse transcriptase. This temperature also a better option to avoid primer dimers and non specific bindings at 48* C. Operating the ABI 7700: [0330] Make sure the following before starting a run: 5 [0331] 1. Cycle parameters are correct for the run; [03321 2. Choice of spectral compensation is correct (off for singleplex, on for multiplex reactions); [0333] 3. Choice of "Number of PCR Stages" is correct in the Analysis Options box (Analysis/Options). This may have to be manually assigned after a run if the data is absent in 10 the amplification plot but visible in the plate view, and the X-axis of the amplification is displaying a range of 0-1 cycles; [0334] 4. No Template Control is labeled as such (for accurate ARn calculations); [0335] 5. The choice of dye component should be made correctly before data analysis; 15 103361 6. You must save the run before it starts by giving it a name (not leaving as untitled); [0337] 7. Also at the end of the run, first save the data before starting to analyze. [0338] The ABI software requires extreme caution. Do not attempt to stop a run after clicking on the Run button. You will have problems and if you need to switch off and on 20 the machine, you have to wait for at least an hour to restart the run. [0339] When analyzing the data, remember that the default setting for baseline is 3 15. If any CT value is <15, the baseline should be changed accordingly (the baseline stop value should be 1-2 smaller than the smallest Cr value). For a useful discussion of this matter, see the ABI Tutorial on Setting Baselines and Thresholds. (Interestingly, this issue is best discussed in 25 the manual for TaqManTM Human Endogenous Control Plate.) [0340] If the results do not make sense, check the raw spectra for a possible CDC camera saturation during the run. Saturation of CDC camera may be prevented by using optical caps rather than optical adhesive cover. It is also more likely to happen when SYBR Green I is used, when multiplexing and when a high concentration of probe is used. 30 Inteipretation of Results: [03411 At the end of each reaction, the recorded fluorescence intensity is used for the following calculations: -86 - [0342] Rn* is the Rn value of a reaction containing all components, Rn- is the Rn value of an unreacted sample (baseline value or the value detected in NTC). ARn is the difference between Rn+ and Rn-. It is an indicator of the magnitude of the signal generated by the PCR. 5 [0343] There are three illustrative methods to quantitate the amount of template: [03441 1. Absolute standard method: In this method, a known amount of standard such as in vitro translated RNA (cRNA) is used; [0345] 2. Relative standard: Known amounts of the target nucleic acid are included in the assay design in each run; 10 [0346] 3. Comparative C 1 method: This method uses no known amount of standard but compares the relative amount of the target sequence to any of the reference values chosen and the result is given as relative to the reference value (such as the expression level of resting lymphocytes or a standard cell line). The Comparative CT Method (AACT) for Relative Quantitation of Gene Expression: 15 [0347] This method enables relative quantitation of template and increases sample throughput by eliminating the need for standard curves when looking at expression levels relative to an active reference control (normaliser). For this method to be successful, the dynamic range of both the target and reference should be similar. A sensitive method to control this is to look at how ACr (the difference between the two CT values of two PCRs for the same 20 initial template amount) varies with template dilution. If the efficiencies of the two amplicons are approximately equal, the plot of log input amount versus ACr will have a nearly horizontal line (a slope of <0.10). This means that both PCRs perform equally efficiently across the range of initial template amounts. If the plot shows unequal efficiency, the standard curve method should be used for quantitation of gene expression. The dynamic range should be determined for 25 both (1) minimum and maximum concentrations of the targets for which the results are accurate and (2) minimum and maximum ratios of two gene quantities for which the results are accurate. In conventional competitive RT-PCR, the dynamic range is limited to a target-to-competitor ratio of about 10:1 to -1:10 (the best accuracy is obtained for 1:1 ratio). The real-time PCR is able to achieve a much wider dynamic range. 30 [0348] Running the target and endogenous control amplifications in separate tubes and using the standard curve method requires the least amount of optimization and validation. The advantage of using the comparative Cr method is that the need for a standard curve is eliminated (more wells are available for samples). It also eliminates the adverse effect of any dilution errors made in creating the standard curve samples. -87 - [0349] As long as the target and normaliser have similar dynamic ranges, the comparative CT method (AACT method) is the most practical method. It is expected that the normaliser will have a higher expression level than the target (thus, a smaller CT value). The calculations for the quantitation start with getting the difference (ACr) between the Cr values of 5 the target and the normaliser: [0350] ACr= Cr (target) - CT (normaliser) [0351] This value is calculated for each sample to be quantitated (unless, the target is expressed at a higher level than the normaliser, this should be a positive value. It is no harm if it is negative). One of these samples should be chosen as the reference (baseline) for each 10 comparison to be made. The comparative AACr calculation involves finding the difference between each sample's ACr and the baseline's ACT. If the baseline value is representing the minimum level of expression, the AACT values are expected to be negative (because the ACT for the baseline sample will be the largest as it will have the greatest CT value). If the expression is increased in some samples and decreased in others, the AACT values will be a mixture of 15 negative and positive ones. The last step in quantitation is to transform these values to absolute values. The formula for this is: [0352] comparative expression level = 2 -Acr [0353] For expressions increased compared to the baseline level this will be something like 23 = 8 times increase, and for decreased expression it will be something like 2-3 = 20 1/8 of the reference level. Microsoft Excel can be used to do these calculations by simply entering the Cr values (there is an online ABI tutorial at http://www.appliedbiosystems.com/support/tutorials/7700amp/ on the use of spread sheet programs to produce amplification plots; the TaqManm Human Endogenous Control Plate protocol also contains detailed instructions on using MS Excel for real-time PCR data analysis). 25 10354] The other (absolute) quantification methods are outlined in the ABI User. Bulletins (http://docs.appliedbiosystems.com/search.taf?_UserReference=A8658327189850A 1 3A0C598 E). The Bulletins #2 and #5 are most useful for the general understanding of real-time PCR and quantification. 30 Recommendations on Procedures: [03551 1. Use positive-displacement pipettes to avoid inaccuracies in pipetting; [0356] 2. The sensitivity of real-time PCR allows detection of the target in 2 pg of total RNA. The number of copies of total RNA used in the reaction should ideally be enough to -88give a signal by 25-30 cycles (preferably less than 100 ng). The amount used should be decreased or increased to achieve this; [03571 . 3. The optimal concentrations of the reagents are as follows; [0358] i. Magnesium chloride concentration should be between 4 and 7 mM. It 5 is optimized as 5.5 mM for the primers/probes designed using the Primer Express software; [0359] ii. Concentrations of dNTPs should be balanced with the exception of dUTP (if used). Substitution of dUTP for dTTP for control of PCR product carryover requires twice dUTP that of other dNTPs. While the optimal range for dNTPs is 500 pM to 1 mM (for one-step RT-PCR), for a typical TaqMan reaction (PCR only), 200 PM of each dNTP (400 pM 10 of dUTP) is used; [0360] iii. Typically 0.25 pL (1.25 U) AmpliTaq DNA Polymerase (5.0 U/pL) is added into each 50 pL reaction. This is the minimum requirement. If necessary, optimization can be done by increasing this amount by 0.25 U increments; [0361] iv. The optimal probe concentration is 50-200 nM, and the primer 15 concentration is 100-900 nM. Ideally, each primer pair should be optimised at three different temperatures (58, 60 and 620 C for TaqMan primers) and at each combination of three concentrations (50, 300, 900 nM). This means setting up three different sets (for three temperatures) with nine reactions in each (50/50 mM, 50/300 mM, 50/900, 300/50, 300/300, 300/900, 900/50, 900/300, 900/900 mM) using a fixed amount of target template. If necessary, a 20 second round of optimization may improve the results. Optimal performance is achieved by selecting the primer concentrations that provide the lowest CT and highest ARn. Similarly, the probe concentration should be optimized for 25-225 nM; [0362] 4. If AmpliTaq Gold DNA Polymerase is being used, there has to be a 9-12 min pre-PCR heat step at 92 - 950 C to activate it. If AmpliTaq Gold DNA Polymerase is used, 25 there is no need to set up the reaction on ice. A typical TaqMan reaction consists of 2 min at 500 C for UNG (see below) incubation, 10 min at 950 C for Polymerase activation, and 40 cycles of 15 sec at 950 C (denaturation) and 1 min at 600 C (annealing and extension). A typical reverse transcription cycle (for cDNA synthesis), which should precede the TaqMan reaction if the starting material is total RNA, consists of 10 min at 250 C (primer incubation), 30 min at 480 C 30 (reverse transcription with conventional reverse transcriptase) and 5 min at 950 C (reverse transcriptase inactivation); [03631 5. AmpErase uracil-N-glycosylase (UNG) is added in the reaction to prevent the reamplification of carry-over PCR products by removing any uracil incorporated into amplicons. This is why dUTP is used rather than dTTP in PCR reaction. UNG does not function 35 above 55 OC and does not cut single-stranded DNA with terminal dU nucleotides. UNG -89containing master mix should not be used with one-step RT-PCR unless rTth DNA polymerase is being used for reverse transcription and PCR (TaqMan EZ RT-PCR kit); [0364] 6. It is necessary to include at least three No Amplification Controls (NAC) as well as three No Template Controls (NTC) in each reaction plate (to achieve a 99.7% 5 confidence level in the definition of +/- thresholds for the target amplification, six replicates of NTCs must be run). NAC former contains sample and no enzyme. It is necessary to rule out the presence of fluorescence contaminants in the sample or in the heat block of the thermal cycler (these would cause false positives). If the absolute fluorescence of the NAC is greater than that of the NTC after PCR, fluorescent contaminants may be present in the sample or in the heating 10 block of the thermal cycler; [03651 7. The dynamic range of a primer/probe system and its normaliser should be examined if the AACT method is going to be used for relative quantitation. This is done by running (in triplicate) reactions of five RNA concentrations (for example, 0, 80 pg/pL, 400 pg/jiL, 2 ng/[L and 50 ng/.L). The resulting plot of log of the initial amount vs CT values 15 (standard curve) should be a (near) straight line for both the target and normaliser real-time RT PCRs for the same range of total RNA concentrations; [0366] 8. The passive reference is a dye (ROX) included in the reaction (present in the TaqMan universal PCR master mix). It does not participate in the 5' nuclease reaction. It provides an internal reference for background fluorescence emission. This is used to normalize 20 the reporter-dye signal. This normalization is for non-PCR-related fluorescence fluctuations occurring well-to-well (concentration or volume differences) or over time and different from the normalization for the amount of cDNA or efficiency of the PCR. Normalization is achieved by dividing the emission intensity of reporter dye by the emission intensity of the passive reference. This gives the ratio defined as Rn; 25 [0367] 9. If multiplexing is done, the more abundant of the targets will use up all the ingredients of the reaction before the other target gets a chance to amplify. To avoid this, the primer concentrations for the more abundant target should be limited; [0368] 10. TaqMan Universal PCR master mix should be stored at 2 to 8* C (not at -20* C); 30 [03691 11. The GAPDH probe supplied with the TaqMan Gold RT-PCR kit is labeled with a JOE reporter dye, the same probe provided within the Pre-Developed TaqManTM Assay Reagents (PDAR) kit is labeled with VIC. Primers for these human GAPDH assays are designed not to amplify genomic DNA; [0370] 12. The carryover prevention enzyme, AmpErase UNG, cannot be used with 35 one-step RT-PCR which requires incubation at 48* C but may be used with the EZ RT-PCR kit; -90- 103711 13. One-step RT-PCR can only be used for singleplex reactions, and the only choice for reverse transcription is the downstream primer (not random hexamers or oligo-dT); [03721 14. It is ideal to run duplicates to control pipetting errors but this inevitably increases the cost; 5 [03731 15. If multiplexing, the spectral compensation option (in Advanced Options) should be checked before the run; [0374] 16. Normalization for the fluorescent fluctuation by using a passive reference (ROX) in the reaction and for the amount of cDNA/PCR efficiency by using an endogenous control (such as QAPDH, active reference) are different processes; 10 [0375] 17. ABI 7700 can be used not only for quantitative RT-PCR but also end point PCR. The latter includes presence/absence assays or allelic discrimination assays (such as SNP typing); [9376] 18. Shifting Rn values during the early cycles (cycle 0-5) of PCR means initial disequilibrium of the reaction components and does not affect the final results as long as 15 the lower value of baseline range is reset; [03771 19. If an abnormal amplification plot has been noted (CT value <15 cycles with amplification signal detected in early cycles), the upper value of the baseline range should be lowered and the samples should be diluted to increase the Cr value (a high CT value may also be due to contamination); 20 [0378] - 20. A small ARn value (or greater than expected CT value) indicates either poor PCR efficiency or low copy number of the target; [03791 21. A standard deviation >0.16 for CT value indicates inaccurate pipetting; [0380] 22. SYBR Green entry in the Pure Dye Setup should be abbreviated as "SYBR" in capitals. Any other abbreviation or lower case letters will cause problems; 25 [0381] 23. The SDS software for ABI 7700 have conflicts with the Macintosh Operating System version 8.1. The data should not be analyzed on such computers; [03821 24. The ABI 7700 should not be deactivated for extended periods of time. If it has ever been shutdown, it should be allowed to warm up for at least one hour before a run. Leaving the instrument on all times is recommended and is beneficial for the laser. If the 30 machine has been switched on just before a run, an error box stating a firmware version conflict may appear. If this happens, choose the "Auto Download" option; [0383] 25. The ABI 7700 is only one of the real-time PCR systems available, others include systems from BioRad, Cepheid, Corbett Research, Roche and Stratagene. -91 - Genotyping Analysis [03841 Many methods aie available to genotype DNA. A review of allelic discrimination methods can be found in Kristensen et al. (Biotechniques 30(2): 318-322 (2001). Only one method, allele-specific PCR is described here. 5 Primer Design [0385] Upstream and downstream PCR primers specific for particular alleles can be designed using freely available computer programs, such as Primer3 (http://frodo.wi.mit.edu/primer3/primer3 code.html). Alternatively the DNA sequences of the various alleles can be aligned using a program such as ClustalW 10 (http://www.ebi.ac.uk/clustalw/) and specific primers designed to areas where DNA sequence differences exist but retaining enough specificity to ensure amplification of the correct amplicon. Preferably a PCR amplicon is designed to have a restriction enzyme site in one allele but not the other. Primers are generally 18-25 base pairs in length with similar melting temperatures. 15 PCR Amplification [0386] The composition of PCR reactions has been described elsewhere (Clinical Applications of PCR, Dennis Lo (Editor), Blackwell Publishing, 1998). Briefly, a reaction contains primers, DNA, buffers and a thermostable polymerase enzyme. The reaction is cycled (up to 50 times) through temperature steps of denaturation, hybridization and DNA extension on 20 a thermocycler such as the MJ Research Thermocycler model PTC-96V. DNA Analysis [03871 PCR products can be analyzed using a variety of methods including size differentiation using mass spectrometry, capillary gel electrophoresis and agarose gel electrophoresis. If the PCR amplicons have been designed to contain differential restriction 25 enzyme sites, the DNA in the PCR reaction is purified using DNA-binding columns or precipitation and re-suspended in water, and then restricted using the appropriate restriction enzyme. The restricted DNA can then be run on an agarose gel where DNA is separated by size using electric current. Various alleles of a gene will have different sizes depending on whether they contain restriction sites. 30 EXAMPLE 2 IDENTIFICATION OF GENES AND PRIORITY RANKING OF GENES [0388] Significant genes were ranked according to an Empirical Bayes approach (Lonnstedt and Speed, 2002, Statistica Sinica 12: 31-46), based on a comparison of all animals -92 at Day 28 compared to animals on days 0, 2, 4, 7, 9, 11, 14, 17, 21, and 24. The empirical Bayes approach was used to provide a shrinkage estimator of the within groups variance for each gene. [03891 Individual p values were based on a t Test using this shrinkage estimator. The p values of the t test were adjusted using Holms method to maintain strong control of the 5 family wise type I error rate. [03901 The genes listed in Table 5 were generated from a total of 783 genes that were significant (p<0.05) across the various days. This gene list was trimmed by eliminating those genes that were significant for less than two days and where p>0.001. The remaining genes were then ranked in increasing order of their p value.. 10 [03911 It should be noted that this gene list is not inclusive of the genes that can act -as diagnostics for stress (see also the minimally predictive set and gene ontology). [03921 The genes listed in Table 6 are ranked in order of their t statistic or value which may be interpreted as a signal-to-noise ratio. The tabulation also displays the log 2 fold change (M value), and the adjusted p values. Genes with a negative t value (and hence a 15 negative M value) are down regulated. Genes with positive t and M values are up-regulated. The priority ranking of genes is based on increasing value of t value for the first day each gene is significant (p<0.001) following stress induction, and for genes that were significant for at least three sampling times. EXAMPLE 3 20 DEMONSTRATION OF DIAGNOSTIC POTENTIAL TO DETERMINE STRESS RESPONSE [03931 The diagnostic potential of the entire set of genes was assessed using discriminant analysis (Venables and Ripley, 2002, Modem Applied Statistics in S, Springer) on the principal component scores (Jolliffe, I.T. Principal components analysis, Springer-Verlag, 1986) calculated from gene expression. Comparisons were made between samples taken 25 immediately after the stressor, and at 2, 4, 7, 9, 11, 14, 17, 21, 24 and 28 days after the stressor. [03941 The entire process was cross-validated. Sensitivity and specificity were calculated for a uniform prior. This may be interpreted as a form of shrinkage regularization, where the estimates are shrunken to lie in a reduced space. [03951 Cross validated estimates of discriminant function scores were then used to 30 construct an ROC curve (Lloyd C.J., 1998, The use of smoothed ROC curves to summarize and compare diagnostic systems, Journal ofthe American Statistical Association 93:1356-1364). The ROC curves were based both on empirical cumulative distribution functions, and on kernel density estimates with a smoothing window chosen using Lloyd's method (loc. cit). -93- [0396) ROC curves for the comparison of each day with Day 28 are shown in Figures 1 to 10, respectively. [0397] Changes in gene expression following transport stress are of sufficient magnitude to produce excellent diagnostic potential. 5 EXAMPLE 4 MINIMALLY PREDICTIVE GENE SETS [0398] Although a large number of genes has been identified as having diagnostic potential, a much fewer number are generally required for acceptable diagnostic performance. [0399] Table 7 shows the cross-validated classification success, sensitivity and 10 specificity obtained from a linear discriminant analysis, based on two genes selected from the set of potential diagnostic genes. The pairs presented are those producing the highest prediction success, many other pairs of genes produce acceptable classification success. The identification of alternate pairs of genes would be readily apparent to those skilled in the art. Techniques for identifying pairs include (but are not limited to) forward variable selection (Venables W.N. and 15 Ripley B.D. Modem Applied Statistics in S 4h Edition 2002. Springer), best subsets selection, backwards elimination (Venables W.N. and Ripley B.D., 2002, supra), stepwise selection (Venables W.N. and Ripley B.D., 2002, supra) and stochastic variable elimination (Figuerado M.A. Adaptive Sparseness for Supervised Learning). [0400] Table 8 shows the cross-validated classification success obtained from a 20 linear discriminant analysis based on three genes selected from the diagnostic set. Only twenty sets of three genes are presented. It will be readily apparent to those of skill in the art that other suitable diagnostic selections based on three stress marker genes can be made. [04011 Table 9 shows the cross-validated classification success obtained from a linear discriminant analysis based on four genes selected from the diagnostic set. Only twenty 25 sets of four genes are presented. It will be readily apparent to practitioners in the art that other suitable diagnostic selections based on four stress marker genes can be made. [04021 Table 10 shows the cross-validated classification success obtained from a linear discriminant analysis based on five genes selected from the diagnostic set. Only twenty sets of five genes are presented. It will be readily apparent to practitioners in the art that other 30 suitable diagnostic selections based on five stress marker genes can be made. [04031 Table Ii shows the cross-validated classification success obtained from a linear discriminant analysis based on six genes selected from the diagnostic set. Only twenty sets of six genes are presented. It will be readily apparent to practitioners in the art that other suitable diagnostic selections based on six stress marker genes can be made. -94 - (04041 Table 12 shows the cross-validated classification success obtained from a linear discriminant analysis based on seven genes selected from the diagnostic set. Only twenty sets of seven genes are presented. It will be readily apparent to practitioners in the art that other suitable diagnostic selections based on seven stress marker genes can be made. 5 [0405] Table 13 shows the cross-validated classification success obtained from a linear discriminant analysis based on eight genes selected from the diagnostic set. Only twenty sets of eight genes are presented. It will be readily apparent to practitioners in the art that other suitable diagnostic selections based on eight stress marker genes can be made. [0406] Table 14 shows the cross-validated classification success obtained from a 10 linear discriminant analysis based on nine genes selected from the diagnostic set. Only twenty sets of nine genes are presented. It will be readily apparent to practitioners in the art that other suitable diagnostic selections based on nine stress marker genes can be made. [0407] Table 15 shows the cross-validated classification success obtained from a linear discriminant analysis based on ten genes selected from the diagnostic set. Only twenty 15 sets of ten genes are presented. It will be readily apparent to practitioners in the art that other suitable diagnostic selections based on ten stress marker genes can be made. [0408] Table 16 shows the cross-validated classification success obtained from a linear discriminant analysis based on 20 genes selected from the diagnostic set. Only 20 sets of twenty genes are presented. It will be readily apparent to practitioners in the art that other 20 suitable diagnostic selections based on twenty stress marker genes can be made. EXAMPLE 5 DEMONSTRATION OF SPECIFICITY [0409] The specificity of a stress gene signature is difficult to define because the test is an assessment rather than a diagnostic. 25 [0410] Nonetheless, the entire set of "stress genes" were used as a training set against a gene expression database of over 850 GeneChipTM. Gene expression results in the database were obtained from samples from horses with various diseases and conditions including; chronic and acute induced EPM, clinical cases of EPM, herpes virus infection, degenerative osteoarthritis, Rhodococcus infection, endotoxemia, laminitis, gastric ulcer 30 syndrome, animals in athletic training and clinically normal animals. The stress status of these animals was not known a priori. [04111 A stress index score was calculated for each GeneChipTm, using the genes in the training set. The score was calculated from a regularized discriminant function, so that large .95 values would be associated with high probability of stress, and the variance of the score should be approximately 1. GeneChipm were ranked on this score, from the largest to the smallest. [04121 Specificity was investigated by varying a threshold value for a positive diagnosis. At each value of the threshold, specificity was defined as the proportion of positive 5 results (i.e. GeneChipTM index score greater than the threshold) which were true positives. A threshold value of two (i.e. two standard deviations) was adopted. [04131 59 animals from the database that were not part of the induced stress trial were identified as having immune modification associated with stress and were two standard deviations above zero on discriminant function when using four principal components and the 10 entire gene set (3105). Of these 59 animals, 10 were in a laminitis trial, 14 had R. equi infection and nine had gastritis. Thirteen animals were "controls," and of these, three had been recently transported, two were in a trial, three were not clinically normal and five were foals with exposure to R. equi. Twelve animals deemed to be clinically normal were identified by the signature as stressed. Based on this information, it can be stated that the specificity of the stress 15 signature is over 90% when used against a database of over 850 samples. [0414] 79 animals from the database that were not part of the induced stress trial were identified as having immune modification associated with stress and were two standard deviations above zero on discriminant function when using four principal components and the unique stress signature genes listed in Table 1. Of these 79 animals, 15 were in a laminitis trial, 20 8 had R. equi infection and 24 had gastritis. Twenty-one were "controls", and of these, 12 were in a trial, and three were not clinically normal. Nine animals deemed to be clinically normal were identified by the signature as stressed. Based on this information, it can be stated that the specificity of the stress signature is over 90% when used against a database of over 850 samples. 25 EXAMPLE 7 GENE ONTOLOGY [0415] Gene sequences were compared against the GenBank database using the BLAST algorithm (Altschul, S.F., Gish, W., Miller, W., Myers, E.W. & Lipman, D.J. (1990) "Basic local alignment search tool." J. Mol. Biol. 215:403-410), and gene homology and gene 30 ontology searches were performed in order to group genes based on function, metabolic processes or cellular component (using UniProt and GenBank). Table 17 lists and groups the genes based on these criteria and information available at the time. See also Table 1, which contains sequence information for each gene. -96 - [04161 The disclosure of every patent, patent application, and publication cited herein is hereby incorporated herein by reference in its entirety. [04171 The citation of any reference herein should not be construed as an admission that such reference is available as "Prior Art" to the instant application. 5 [04181 Throughout the specification the aim has been to describe the preferred embodiments of the invention without limiting the invention to any one embodiment or specific collection of features. Those of skill in the art will therefore appreciate that, in light of the instant disclosure, various modifications and changes can be made in the particular embodiments exemplified without departing from the scope of the present invention. All such 10 modifications and changes are intended to be included within the scope of the appended claims. -97 - U) UUHPE 0vu i <. 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U E 0 04E El t- E4 LI -4E-4W -41CE44E -4 E- 4E S E 1 E-4 Vt -V WV LVV U _)L E4- 44U. V E4 H V Uo0 4V uDE- V ~E-4 0P-iD0 04 E-4 - 44 L)VU 0 uCH 0 4 4 V u )9 F - E4 4 4 -4 E440 0U44E1 E-4 H ~ 0 E-0 U 0 U U V U L) E- E1- L) E1-4~~ 1 W 2-E' 1E- ' VE0W1 W 1-' 4(uU L) E4 U E)4D ~E4- ' 4 VO V E-1W U U gE~V #F:C W E-4~ U ~ E-W WW'-' V- 4 U W 4- E-E- O CD -4U0 f-4C L)1-E. W D V o it u - E4 UD4-~ WVV 4 4 U 4 E-4 P V 8W )-1- E-4 o L)vDW VWVE-4 - L E-FC D~V .)V W W -V Q) C.)E W~ '.4 . 4. . I UPu U E- El 0 V P WV <-V E- HH44VMUE-~ W 1 14 VWO4M 4 :9uu E'E- ' I-l E- ~ EV UD B DL WMC E 14 V W~ E V - E-4D V-V ~V E4M ~ E- M E- E4E E-4 94 u u E- E-4 sL 8uu VE-' ' E-4 U- L) - VV CD I- HU EW E .~ 6. '4 -4 Eu Uo E8 L U U1

-

L , H E-4 EAE uH4u )) E4 U o ~ ~I E.P - Hu U) 0N z U) L) I U U 4 U 4U WU= 0C EA4 0 U F4L u 0E4 CD rE-4 E4 W 0) > 4 U W W 0 64 ML ) 0 04 I 1 E4 1 E-4 6 E- ug w) L) P 6E UU W I. X.E. ) 04U OE. 6 E-U - 4E4 >E E- U 0 14 > E- 0) u u0 V E-4 U Q) a# . u >E )o4 8 N g E-4E- >:C U~ 0E. L) 0 8 aaE o

U

8 8 u. C.) U E- EC.)0 H E-'N ) 4U V)l 0 > E-4 U D >E-4 XE-' E-4 cij N-. ()P 8 E fl E4 u4 Ua * I.0 U L) p U S 'o~ E4U0 OU8 u8u 6 W uU 6 u 14 U UU U U UE- U E- 8U 2 ) ocL E-.UHH - 00 C-4 bN 0 0 4 NW O -4 - -4 N. U-C ,4~ EU 4~ u 4 .- 41 N8 u W N1 NnL E-E 7 L

EVE

L)0 L PC Q 0 > 1 E-4 U E E 4 0->p > E 0 9 0 -. E4 C, z 0o w ra ft l (d U U 4. 0 0 1 fd (0 I 1010ON(0 1V0 7%040 4) id 04 3 -' - Uo t104M.310U U (U1CO 0 V it 0 (0 U 0 0 M 10104) 0 t100U() CO M V 4J U J(0 4- 4.) V W Vt u 4 c UON4d(d4 ) 01 0 100(0 pt%($tCCdr dVMr 4.1V(0 1 04M M0CC 0400%4-) 040 00(C(4U 4.O)V O 100(d U M U0010 (0 ( U1CCV44-) r0- L) tptM U 4J4.)0(I V 10 Vtl M4 4014( U CC V U U rd U01 U 0 u CD ~ 0401(a 1 (d(dONmtov' . (( ro V UV( ' fd4J (d 14 P 0 4.) V E 4 ( J M 0 4(( 0 0 1 t1 0 1 0 4 J t 1 0 ( 4 U , V 4 J W V CO 0 4 1 4 C 0 U ( 0 14 J0 04 m a) 4(1100al 0 m 0 0 V P M U 01 r VCO4 M01 L V01 aE 41I-' C (C( 10((1 4J .)101 M4J41 0U 1 d0-1 M 4.44.34. 1 00(M V V1 P )4 ac C dVa di IME- WW U0 401014 4. 04( 04 MId 0 1 4J 0(40 OU M(d V4 4.) 0 V 0- 1-. (0 101 100 J0 001 0(0 M( 0UV0(04 c 04 CU VV V 0 U u 0 r U C 010 (44(( 4 1 010U(4 M Id10 Id IM 404((10 M UVUI 1 . O( f'.! 4~~~01 J r V 4) U C 4.) 01 0 4 04f(0 COId O 10 4. V (d0 4J (10 q~~ 0 0 U V 4J CC VM0U1M U U10010100tM4 Mb MUM (1104J 41 M t tr 0 M-4 4Jl 4(J0(4 1 1 0 (0 (d 4-)UlU4-)4-4( 01 0 U LD u- U. 0 4) 0 4. 4 4 U 4-) 0(10 Ot4.J01 04 00(0 ((0 4 :H 9c P 10104 o00(00(t(000100U1004. U4) Ci MV4-)0( M(00( M( V10 01 010 0 u ) ( WVU U0 01000104 U1M N0U0V(04(d0 (d 0 U(d010V (1 01040 U )t J V? W 4J M )4 -4 UU4 0VV4)( 40 4 c (d 4(d00(4 i10U 4J U (10 fd(d(d UM M UC-VU0 4. 4 ) V bi V10 Cflm m 10 (d u bi l go uol (d a - 10 to V 010-a u alto1v1V4.) 1 0r LD al4 H U 0% 0 0 I(d M V V0104 V CC Urd U VV U 4 1 1 CC UV0it01M0V(4.)( Q 04 C 0)4D~ 0 -40 4) tom(a010d 01 J(0 tn M4 11000 0(0 (0 0 4-)%.)( d d0 Mc 0144)11 0-4 Id lu C 0aUbir U U 40101441 (((0P i NM4.)M JU 4JCU UN 0 U10 10 V4 M E 4, a v44 10 4.) 0014110%.t JIMIMU 4(1 4.)0UV10%0U 1O(0U4.J M C CC V0 V L 40 b El 01(0 4J 4-310) 4J t4.34.) IM4 1 4.10M 0 .M4.) C U 4 V410V10 E 0 Lo 0 tJ4 MV( 0( 4.) IM M( IV V 01 (01 U 0% (10 0 V4) $4 C 9 0 I~l 4 uumul w z 010 01 0 . 0( 01 10 V 414CO4W0 U M (4( (d0U4V0M4k 40-. 0 ) ) 0 to Cd U 1 4-J M fO (0(4) U M IM V r CU CC U U f U V rd 011V 0 0 a & (D > 4JMC U 01 4J CC M (0 U 4J 00 0 10 V U M U (d TO V0 M CC M . G 0-' (0 040 E 0 - 0(~ 104(1Vcd04U(01400(0M0(104(00V1M(4.0 (0 U U004(d((( U UOc 0 d tD 0 0 CO V U C (0d 0IM N. (d 1743 01 NA IM 0 U NC M 0 N V WM0 P LU O LOD Z Vtn 0 C 01(d f V 1 U4J (d4J V - (4 U IM V4 (d V~ V4 V V- CC a)r V F:C~ ~~ 4 - c4 dI 01 i4 JMCC0VVUVUVUVVMUUVt J E E u u 0~~~~~~~~1 4 d4)V 1UVUV0U0V Jr OU( dr U E4 Q 0: tq uM d O d(dt% ~mb MUtpV4. d OL)M4. MC 4)c40 Uf u I t tl(dUrU( ( V C UV U JU 0COUONU ~ t%4-.' dM u ) >E- A - .,m 4 U ( UId(0M -JU 4 4 tl d-WL)U J V ~lOnV 0V CJ 4 Qol4JIMON4JONM d P f f ( 4J430 4J l U U -)0 -J4- ( 4) O L)~~ ~ ~ H , M4)4)MVC dua lO o'Vt ac auVr . - ~ 4 44 EnuUV UU ardc l lr uva Vmut) ototm 0oV E EAz t d0 d( ~ C( JU(0t - 34 l0 CVU4 . 0 7 u4 aC 11r 1 %4 V MUUf - JV( rO N ~ JV U )U41V( 14 suV I 1V4 y 1t . I 4 14r 1 1 H1 0 a( omo %O a4.1 oU; a0 ,4 CU( ) 0C . 1 r co~~ ~ ~ OA1 -W C C4k L9 E4 4) L) ~ ccF U23 Q~ ZC z 4 0 OCH3 - >4 9 ) A ,4 020 ju H u E-4 E4 U H 4 H 0L E4 0 D D 4 H o cu 4 u pD 4u 4 a0 A E->4 >4 0 >4g 4~ >3 A . P6- W2 0~ W 6 E'IZ'pH .- 4 CO2 E E- U D 0 0 H 0~E LHCDH > CD CD H -U 4 ZH 4W F4 en.6 E-' 4 E- 0 4 WL E'4 N LO' g 3 ,) >U4 Z E4 0 0 Z 4 C4n u~ A >E1249s 0 04 0 4 92 o2 z2 Wu >u U u~ HO ZqH cEW 0.W 4 H )L 4 E4 E- E i ~ ~ - U H CDH a 014 0*0 UW >2 HO 4 A E-4 m 9 - A ~ E4~ U ~ -D u u en4 >6WD N ~ >~ o E-4 L) -4 4 -4H E40 CD U n( / O P - H H- XUl H E-1C HA H4 UD H E- 4 D 0D 8 - U~ E-4 W~ E-43 04 02f Q2 LD 0H Z-4 44 H- H- H U H6 u H 4a: 021 >~ E4~ A E>1 3: 02 p2 Ht>4 ~ en H r4 CD 4E4U 4 64 .- 4 N D 6-4' ui ,-4 p4 i-h pW N r r '0 n' m O ~ 0 W ~ N LW cw 0 W ~ O 0 N E4I4 4 L - - gc n C U 4 8 >E 8 . E, EH-342- 0 0 0 z z 0 Hi C) U) '1,1 4> . W.Lo L o~ L4 E 4- C. Ei~ ~ E-4 -4~ W'I u 00 1. E - 1-1.U - E4- L)W U u E Uz 0 H~ -1 CE4 WU43 14 U 1 > E- AW E-1 0E- U ~ 1 E -4 U E-4 L) ~ ~ W E-' 1 U4E-1 14UWI-01 UU H ) 0U ) p -4E-40 H U -iU - 1-413 E LI)U 0Hu UWE-44 g E4 L) u H El E. 18) H 1. 8E--0U - fl 13 0 . 3 L9 13 0, E-1il- o3 L) t -40 E4 H-E4 0 U H U U C ~ I' .E EA E L). U)1~ - - U) 1- 4 E-i H 1 ~10 EA H3 E w -343O ~ '4-' w - E-4 UE-4~ E-44E-1 § ULD U- 0 0 E-14U 0' L) U) )U0 U3 P , U 8- UE41.3U -U E-$ 31 1 0 W- E - i 0 4 -4 3 I- I-AU - 13 *U Q~ -4 ~ Es -E-4 u U6 -1 E-1 AE' HIi E4 U~ E- 00 NW 0' C) U~ H Hq.0WNuW(W N E 0 ) 0 ) E ~ ~ ~ 5 0 E E ~~ ~~~ 0 -d 0-i 8U0 -u E ~~~~ O af l0D F:4~' E. 4-4E N-4 UE4 4L E. E- H E4U E L) >4 4 4 A u 64 0 E4 A p D 40 L - zH 44 L0 C. E-EA E-1 u u C.)) El I8j 4-1- H 1-. C) C.) EU u 0U a . w Z I E44 L) 6 E4E uIC . 004 4'4 M'CL) E E- -4 .48 (4 .4' -I -~ uIiFC E-44 TABLE 2 .'Probe: Set Name *;,- PROBE SEUNEsequence". identifier. Pleckstrin B1960933.V.3_at ACTTGAGAGGCTGCGTGGTGACTTC SEQ ID NO:250 B1960933.V1.3_at GCCCCTGGGAGCGATTCACTTGAGA SEQ ID NO:251 B1960933.V.3_at GAATTTTCATCTGGCAGGGTTCCGA SEQ ID NO:252 B1960933.V1.3 at GAACCTCTTTGAGATCATCACGGCG SEQ ID NO:253 B1960933.V.3_at GAATTCCAGCGATGATGACGTGATT SEQ ID NO:254 B1960933.Vi.3_at GAAQACCCTGCATATGTGCACTACA SEQ ID NO:255 B1960933.V1.3 at GTTCATTATTTCTTGCAAGCGGCCA SEQ ID NO:256 B1960933.V1.3_at GGATAAACTCGGTCCAGGGCCTGTC SEQ ID NO:257 B1960933.Vl.3_at GTGACTTCAGTGGAGGGCAACCCAG SEQ ID NO:258 B1960933.V1.3 at GGGCCTGTCCACTTCTGGTGACAAG SEQ ID NO:259 B1960933.V1.3_at GGAAGTGAGGGCACACCTGCAGCTC SEQ ID 110:260 G protein-coupled receptor HM74a __________________ B1961009.V.3 at AGACAGGTATTTCCGGGTGGTCCAT SEQ ID NO:261 B1961009.V1.3_at AGCATCATCTTCCTCACGGTGGTGG SEQ ID NO:262 B1961009.V.3_at AATCCAGCCGGATTTTCCTGTTCA.A SEQ ID NO:203 B1961009.V1.3_at AATGGCCTTGCCCTTTGGATTTTCT SEQ ID*NO:264 B1961009.Vi.3 at GAAAAACTGCTGTGTGTTCCGGGAT SEQ ID NO: 265* B1961009.Vi.3 at GTTCCGGGATGACTTCATTGCCAAT SEQ ID NO:266 B1961009.V.3 at GGATCATGCTCTTCATGCTGGCCAT SEQ ID NO:267 B1961009.V1.3_at TGGATTTTCTGTTTCCACCTCAAAT SEQ ID NO:268. B1961009.V1.3_at TGACTTTCTCTTGATCAT!CTGCCTA SEQ ID NO:269 B1961009.V1.3 at TCCTGTTQAACTTAGCCGTGGCTGA SEQ ID NO:270 B1961009.V1.3 at TAGGTGAGGAGCTCCCTAGGACGAG SEQ ID NO:271 B1961185. .3at ATCTCCATCTGCTA CTTCGAGCAG.G SEQ ID NO: 272 B1961185.V1.3_at AGTGGGTCAAGGTGCACGAGCTCAA SEQ ID NO:273 B 1961185.V1.3_at CGAGAGTAACCGCATTGTGACCTGC SEQ ID NO:274 B1961185.V1.3_at ACAGCTTCCTGGTGGAGCCCATCAG SEQ ID 140:275 B1961185.V1.3_at ACAAGTTCGCTGTGGGCAGCGGCTC SEQ ID 140:276 B1961185.V1.3_at AACCACGAGGTGCACATCTATGAGA SEQ ID NO:277 B1961185.V.3_at AACGGGCAGGTGACAGGCATCGACT SEQ ID 140:278 B1961185.V1.3 at AAGGAQCGCACACAGATTGCCATCT SEQ ID NO:279 B1961185.V.3_at GCAACGCCTACGTGTGGACGCTGAA -SEQ ID 14:280 B1961185.V.3_at GTGCAAACACATCAAGAAGCCCATT SEQ ID 14:281 B1961185.V.3_at GGACGCTGAAGGGTCACACATGGAA 'SEQ ID 14:282 PREDICTED: Homo sapiens steroid receptor RNA activator 1 (SRA1)_________ :B1961443. .3 at TGGGAGGCCTTCTCTAATTTGGCTC SEQ ID NO: 283 B1961443.Vi.3_at AGGCTCCATAATCCTGTGGGTTCCC SEQ ID 14:284 B1961443 .V1.3_at ATGTGATGACATCAGCCGACGCCTG SEQ ID NO: 285 B1961443.V.3_at ATGGCTCTGCTGGTGCAAGAGCTTT SEQ ID NO:286 B1961443.V.3_at JAGGAGCACCAGACCGTACCAGGCAT ISEQ ID 140:28 -345- 1 Identifier. B1961443.V1.3_at AAGAGCTTTCAAGCCACCGTTGGGA SEQ ID NO:288 B1961443.V1.3_at AAGAGGAGCCTGTCTTCAGAGGAGA SEQ ID NO:289 B1961443.V1.3_at GCATTGGACGATTGCCGTGGCCACA SEQ ID NO:290 B1961443.V1.3_at GAAGAGAAATCTACAGCCACAGCTG SEQ ID NO:291 B1961443.V1.3_at GGGAAGCTGTCAACGCCTGTAAAGA SEQ ID NO:292 B1961443.V1.3_at TTACCACTTTGGAGACTGTCTGCCC SEQ ID NO:293 HREV107-3 B1961494.V1.3_at AGTGCCCCGCAGCGACCAGGTCAGA SEQ ID NO:294 B19614-94.V1.3_at CAGCGACCAGGTCAGAGACGCCATC SEQ ID NO: 295 B1961494.V1.3_at GCCCCGCAGCGACCAGGTCAGAGAC - SEQ ID NO:296 - B1961494.V1.3_at GCAGCGACCAGGTCAGAGACGCCAT SEQ ID NO:'297 B1961494.V1.3_at GAGTGCCCCGCAGCGACCAGGTCAG SEQ ID NO:298 B1961494.V1.3_at GTGCCCCGCAGCGACCAGGTCAGAG SEQ ID NO:299 B1961494.V1.3_at TGCCCCGCAGCGACCAGGTCAGAGA SEQ ID NO:300 B1961512.V1.3_at AACTCAGAAGACAGAAGTACAGGAA SEQ ID NO:301 B1961512.V1.3_at GCGCAGGAAAGGTGATTTGAAGCCT SEQ ID NO:302 B1961512.V1.3_at ATAGTAATTGGGAGTGGCAGGATAA *SEQ. ID NO:303 B1961512.V1.3_at ACCTTCATGTTCGTGGCGCAGGAAA SEQ ID .NO:.304. B1961512.V1.3_at AAGATAAGACGCCTCTAGAAGACAG SEQ ID NO:305 B1961512.VI.3_at CCTAGTTGGTCTTATGGCATTATTT SEQ ID NO:306 B1961512.V1.3_at GACGCCTCTAGAAGACAGAAACTAA SEQ ID NO:307 B1961512.V1.3_at GAGACCTTCATGTTCGTGGCGCAGG SEQ ID NO:308 B1961512.V1.3_at GTGATTTGAAGCCTAGTTGGTCTTA SEQ ID NO:309 B1961512.V1.3_at GGTCTTATGGCATTATTTGCTAAAA SEQ ID NO:310 B1961512.V1.3 at TTCAAACCCAAAAGGTAGGAAGCAG SEQ ID NO:311 B1961539.V1.3_at ATATCATGGAGGACCTGGATACCAA SEQ ID NO:312 B1961539.V1.3_at ATCATCAATGTCTTCCACCAGTACT SEQ ID NO:313 B1961539.V1.3_at ACGGCCACAGCCACTAATCTGGAGG SEQ ID NO:314 B1961539.V1.3_at CAAGCAGCTGAGTTTCGAGGAGTTC .SEQ ID NO:315 B1961539.V1.3_at GAGCTGGCGAACTTCCTCAAGAGTA SEQ ID NO-:316 B1961539.V1.3_at GATGCACGAGCATGACCAAGGCCAC SEQ ID NO:317 B1961539.V1.3_at GAGGAGTTCATCATCCTGGTGGCCA SEQ ID NO:31-8 B1961539.V1.3 at GGAACTGTCCCAGATGGAGCGCGAC SEQ ID NO:319 B1961539.V1.3_at GGAGAGTGGCCATGGTCACAGCCAT SEQ ID NO:320 B1961539.V1.3_at GGAGCGCGACATAGAGACCATCATC SEQ ID NO:321 B1961539.V1.3_at TGACGCATGCCTCCCATGAGAAGAT SgQ ID NO:322 ILT11A mRNA for immunoglobulin-like transcript 11 protein B1961620.V1.3_at AGGACGTGACCTACGCCCAGGTGAA SEQ ID NO:323 B1961620.V1.3_at AGGGACCCCAGAAGACATAGGAGCT SEQ ID NO:324 B1961620'.V1.3_at AGGTGAACCACTTGACCCTCAGAGG SEQ ID NO:325 B1961620.V1.3 at AGTGGTACGCTGCTATGGCCATCCA SgQ ID NO:326 B1961620.V1.3_at AGCAGAGCCCAGTGGTACGCTGCTA SEQ ID NO:327 B1961620.V1.3_at CATAGGAGCTGCCTCCAGAGGACAC SEQ ID NO:328 B1961620.V1.3_at GAGACTGCAGGGACCCCAGAAGACA SEQ ID NO: 329 - 346 aSna e PRB EUEiCE' Sequence '~, .,' ~ ,. . Identified B1961620.V1.3_at GATGCCACCCTCCATGGAGGGAGAC SEQ ID NO:330 B1961620.V1.3_at GTATGCACAGGCTGCTATATCTGAA SEQ ID NO:331 B1961620.V1.3_at TGGCCATCCACTAGCCCAGGAAGGA SEQ ID NO:332 B1961620.V1.3_at TAGCCCAGGAAGGACCCGGATGCCA SEQ ID NO:333 Mn-SOD mRINA for manganese superoxide dismutase B1961637.Vl.3 at AGATTGTTGCCTGTCCTAACCAGGA SEQ ID NO:334 B1961637.V1.3 at GCATTATCGTTACACCGAGTGCATT SEQ ID NO:335 B1961637:'V1.3_at CGTGACTTTGGTTCCTTCGACAAAT SEQ ID NO:336 B1961637.Vi.3 at GCAGCCTGCACTCAAGTTCAAiTGGT SEQ ID NO:.337 B1961637.V1.3 at GAAGTTGACTGCTGTATCGGCTGGT SEQ ID NO:338 B1961637.V1.3_at TAAGGACCAGGGACGCCTCCAGATT SEQ ID NO:339 B1961637.V1.3_at GGAGGCCATATCAATCATACCATTT SEQ ID NO:340 B1961637.V1.3_at GGM CAACAGGTCTTATTCCCCTGC SEQ ID NO:341 B1961637.V1.3_at GGAGCACGCTTATTACCTTCAGTAT SEQ ID NO:342 B1961637.V1.3_at TTGCTGGACGCCATCAAACGTGACT SEQ ID NO:343 B1961637.V1.3 at TTTTCTGGACAAACCTG4GCCCCAA SEQ ID NO:344 B1961648.V1.3 at ATATGAGGAGCTGAACCTGCCGGCT SEQ ID NO:345 B1961648.V1.3_at GGGCTCATCGAGCAGTACGCTACGC SEQ ID NO:346 B196164B.V1.3_at AGGAAGACAGTTACAGCCGCCTTAT SEQ ID NO:347 B1961648.V1. 3 at AACAGCGCCAGATCCTGCAGGAGAA SEQ ID'NO:348 B1961648.V1.3_at CAAGACAGCTTTCTATTCCTTCTAC SEQ ID N~O:349 B1961648.V1.3 at CTGGCTGGTGGTTCAGTGTCTGCAA SEQ ID NO:350 B1961648.V1.3_at GACGGGCAAGATTGGCACTGACATC SEQ ID No:351 B1961648.V1.3 at GGGCGAGTTCTTTCAGATTCAGGAC SEQ ID NO:352 B1961648.V1.3_at GGACGATTACCTTGATCTCTTTGGG SEQ ID NO:353 B1961648.V1.3 at TGCCGGCTGTGTTCCTGCAGTATGA SEQ ID NO:35.4 B1961648.V1.3_at TTCCTGTAGCTGCTGCCATGTACAT SEQ ID NO:355 NAD synthetase 1 B1961671.V1.3_at AGAGCTGGAGCCCTTGACCAACGGA SEQ ID NO:356 B1961671.V1.3 at AGAAAACCAGGTTCTCCAGCTCGAG SEQ ID NO:357 B1961671.V1.3 at ACGGCGTGGTCAGCAAGTCTTGTTT SEQ ID NO:358 B1961671.V1.3_at AAGACCGGGCCCTATAGCATGTTCT SEQ ID NO:359 B196167-1.V1.3_at GAAGTACTCCGCGAACAGACACAAG SEQ ID NO:360 B1961671.V1.3_at GACAACAGGTTCGATCTGCGGCCAT SEQ ID NO:361 B1961671.V1.3_at GACCAACGGACAGGTGTCGCAGACT SEQ ID NO:362 B1961671.V1.3_at TGAAGCGGTTTTTCTCGAAGTACTC SEQ ID NO:363 B1961671.V1.3 at GTGGCAGTTCCGGTGCATAGAAAAC SEQ ID NO:364 B1961671.V1.3_at GGATGACGTACGCAGAGCTCTCCGT SEQ ID NO:365 B1961671.V1.3_at TATAGCATGTTCTGCAGACTCCTCA SEQ ID NO:366 B1961682.Vl.3_at ATATGGGCCCCGGTATGCAGTGCAA SEQ ID NO:367 B1961682.V1.3_at CGTGGCAACCGCAAGTCTTTGAGGC SEQ ID NO:368 B1961682.V1.3_at AGAGGCATGGTCCAGAACAGCTCCC SEQ ID NO:369 -347- ~. PROBE: SgIQ ,. .*,, eqnco! B1961682.V1.3_at AGAAGAATCCCCAGGCTCCAGTTTA SEQ ID NO:370 B1961682.V1.3_at AAGCCTGAGGACACCACACATGGTC SEQ ID NO:371 B1961682.V1.3 at TCCAGTTTACCCAGTGACACTTCAG SEQ ID NO:372 B1961682.Vi.3_at. GCTGCCTCCAGGACATCTATATGGG SEQ ID NO:373 B1961682.V1.3 at GCATGAAGATTCTGCTCACCAGCAA SEQ ID.NO:374 B1961682.Vl.3_at GACTGAGCAAGGGTTCTGACCTGGA SEQ ID NO:375 B1961682.Vl.3_at GAGA-TCATGGACCTGCTAGTGCAGT SEQ ID NO:376 B1961682.V1.3_at TTAGCTGCTCGAGAACGCAAGCGTT SEQ ID NO:377 No Homology B1961711.V1.3_at CCGTTCGCGTGCACCCAGGGAGGAC SEQ ID NO:378 B1961711.V1.3_at GTCGCCGTGGTCACCCACAGGAAGG SEQ ID NO:379 B1961711.V1.3_at CAGCCTGGGTTTTCTCGGGCGGCTC SEQ ID NO:360 B1961711.Vi.3_at CATTTTCTTCTGGTCGCCGTGGTCA SEQ ID NO:381 B1961711.V1.3_at CAGGTCTCAGCCTGTGAGGACTGCG SEQ ID NO:382 B1961711.V..3 at GACTGCGGCGAGTCTGGAGACCCCA SEQ ID NO:383 B1961711.Vl.3_at GA GGGCCATCTGCTGACAGAGCAAC SEQ ID NO:384 B1961711.V1.3 at GTGTGGACCCACGAGGGCCATCTGC. SEQ ID NO:385 B1961711.Vi.3 at GTGGGCTCTGTCTGGTTCACAGAGC SEQ ID NO:386 B196J.711.Vi. 3 at TGCACCCAGGGAGGACTCGGAGTCC SEQ ID NO:387 B1961711.V1.3_at TCTTCGGGACTGTGTGGACCCACGA SEQ ID NO:388 Tumor necrosis factor inducible (TSG-6) mRNA fragment, adhesion receptor CD44 putative CDS B1961885.V1.3 _.at AGGTTGCTTGGCTGA.CTATGTTGAA SEQ ID NO:389 B1961885.V1.3_at ACTCAAGTATGGTCAGCGTATTCAC SEQ ID NO:390 B1961885.Vi.3_at AATGCGGTGGCATCTTTACAGATAC SEQ ID NO:391 B1961885.V1.3 at CTAAGCGATGCTTCGGTGACCGCAG SEQ ID NO:392 B1961885.Vi.3 at GCGTATTCACCTGAGTTTTCT.GGAC. SEQ ID NO:393 B1961885.V1.3 at GAACCCCTTTGATCTCAGTTTTGTA SE6 ID NO:394 B1961885.Vi.3_at GTGACCGCAGGAGGTTTCCAAATCA SEQ ID NO:395 B1961885.V1.3_at TTTTAAATCTCCAGGCTTCCCAAAT SEQ ID NO:396 B1961885.Vi.3_at TAACCAAGTCTGCTACTGGCACATC SEQ ID NO:397 B1961885.VI.3 at TACAAGCACTACTTCTACGGGAAAT 'SEQ ID NO:398 B1961885.Vl.3_at TATGGTTGTCTCTTTTGGAACCCCT SEQ ID NO:399 Fibroblast; mRNA for aldolase A B1961941.Vi.3 at AGGGCTTTAGGCTGTTCtTTCCCAT SEQ ID NO:400 B1961941.Vi.3_at AGGAGGAGGCATCCATCAACCTCAA SEQ ID NO:401 B1961941.Vl.3 at AGTGGAGGTATTCTAAGGCTGCCCC SEQ ID NO:402 B1961941.Vi.3_at AAATACACCCCAAGTGGTCACGCTG SEQ ID NO:403 B1961941.Vi.3_at TGAAGCCCAATATGGTAACCCCAGG SEQ ID NO:404 B19619.41.V1.3 at GATTGCCATGGCAACTGTCACGGCA SEQ ID NO:405 B1961941.Vi.3_at GTCTGTGGTATTGTCTGTGTATGCT *SEQ ID NO:406 B1961941.Vi.3_at GGAATATGTCAAGCGAGCCCTGGCC SEQ ID NO:407 B1961941 . V. 3_at iTGGGATCACCTTCCTATCTGGAGGC ISEQ ID NO: 408 -348- P. . PROE 4'* -Sequence>. B1961941..Vl .3_at TTGCCTCCCTGGTGACATTGGTCTG SEQ ID NO: 409 B1961941.Vl.3_at TTCATCTCTAACCATGCCTACTAAG SEQ ID.NO:410 High-risk human papilloma viruses E6 onooproteins targeted protein E6TP1 beta mRNA __ BM734457.Vl.3_at ATGATGACTGCACCCCACGGAGGAG SEQ ID NO:411 BM734457.Vl.3_at AGGCCCTACGGCTATGCCTGGCAGG SEQ ID NO:412 BM734457.Vl.3 at AGGAGTTGCTCTGAAACCTACCGCA SEQ ID NO:413 BM7344 57.Vl.3_at AGATCTGCAAGGTGGCAGTGGCCAC SEQ ID NO:414 BM734457.Vl.3_at ACCCCACGGAGGAGTTGCTCTGAAA SEQ ID NO:415 BM734457.Vl.3_at CACGGTGAAGGTGGTCATTATCCCC SEQ ID NO:416 BM734457.Vl.3_at AACCTACCGCATGCCAGTGATGGAA SEQ ID NO:417 BM734457.Vl.3_at CTGCTGAGAACATCCGTCACGGTGA SEQ ID NO:418 BM734457.Vl.3 at GATTGATCTGCTGAGAACATCCGTC SEQ ID NO:419 BM734457.Vl.3_at GGCAGTGGCCACTCTGAGCCATGAG SEQ ID NO:420 BM734457.Vl.3_at TGAGCCATGAGCAGATGATTGATCT SEQ ID NO:421 No homology'_______ BM734531.Vl.3_at ACCACTTCATGTTCTOTACAGAGCT SEQ ID NO:422 SM734531.Vl.3 at ACAGAGCTGTCCAGAGCCGAGGCTG SEQ ID NO:423 BM734531.Vl.3 at AAACGAGTCCGAGGGCACAGCCAGG SEQ ID NO:424 BM734531.V1.3_at CGTTGCCCGCTGTTGGTCATGACAA SEQ ID NO:425 BM734531.Vl.3_at GAGTCTCTGTCAGGATCCTTTTGAA SEQ TD NO:426 BM7 34531.Vl.3_at GAGTCACCCAAGGAACTTATGCAGA SEQ ID NO: 427 BM734531.Vl.3-at GTCCTGTGGCTTTTGTGTGTCTCTC SEQ ID NO: 428 BM734531.Vl.3 ,at GGCCTTGCTTGAGAGAGGTCCATCC SEQ ID NO;429 BM734531.Vl.3_at GGTCACTTAGCAGCGACTTCTTGGA SEQ ID NO: 430 BM734531.Vl.3 at GGAGCCAGGTGTCTGCATTTGAACA SEQ ID NO:431* BM73453.-.Vl.3 at TTATGCAGATGGCATGTCCTCACTC SEQ ID NO:432 No homology BM734654.Vl.3_at ACCTAGACGACCTGTCGGGATTGAC SEQ ID NO:433 BM734654.V1.3_at 'CGATTCCGTTATGCGGTCCAAGCAA SEQ ID NO:434 BM734654.Vl.3_at TGAACGGGACCAGCCAAACGACGGG SEQ ID NO:435 BM734654.Vl.3_at AGAACTTCTCATGCTTCATCTACAT SEQ ID NO:436 BM734654.V1.3_-at GACCGTGATGGTCAACACCAGCCAA SQID NO:437 BM734654.Vl.3_at GACGACGTCCAGTATTTCCTGTATA SEQ ID NO: 438 BM734654.Vl.3_at GGGATCCAGTTCTTCGATTCCGTTA SEQ ID NO: 439 *BM734654.vl.3 at GGAATGTCCCCGTTACATGAGCGAC SEQ ID NO:440 B1734654.Vl.3_at TCTACATCGTGCACTTCATGATCTG SEQ ID NO:441 BM734654.Vl.3_at TTTCGGAGAAGCTCGTCTACACCAA SEQ ID NO442 BM734654.Vl.3_at TTGACCTCTTACAATTACTTCGTGG SEQ ID NO:443 Nohomology BM734719.vl.3_at ACGCCAATGGGTCAAACTAACTCTG SEQ ID NO:444 BM734719.V1.3_at AGAAGTCCTCTCTGAGACTCAAGGG SEQ ID NO:445 BM734719.V1.

3 _at AAAGCCCATGAGCTGCTTCTTTGTT SEQ ID NO: 44'6 BM734719.Vl.

3 _at AAAAATCTCTCATCCTATTCTGCTT SEQ ID NO:447 -349- ;? . ,e PROBE SEQ.N _B 'Seqec* _______________________ 7 .. .. Ideintif ier BM734719.V1.3_at AAGCCTTCCTAAAAGCAd-A TTGCC SEQ ID NO:448 BM734719.Vl.3_at AAGGGCTAAGGCA.AGGTCTTCCAGA SEQ ID NO:449 BM~734719MV.3 at CAAGAAATGACAGCCTCCAAGCCTT SEQ ID NO:450 BM734719.V.3_at .GAAGCTTCTTCCCACCTAGAGAA SEQ ID NO:451 BM734719.V1.3_at GGTGACAACGCTGGCTGCTGAAAGC SEQ ID NO:452 BM734719..V1.3_at TTTCCACTGTCGTCAGAGCCAACAA .SEQ ID NO:453 BM734719MV.3_at TTCTTTGTTCTCTGTCACGGGACAA SEQ ID NO:454 No homology BM734722.Vi .3_at CGGGCGACTCGCAGAATCAATACAT SEQ ID NO:455 BM734722.V.3_at ACAGAGCCCCGGTCAGCGGGTGAAA SEQ ID NO:456 BM734722.V.3_at AACTGAACGATAACCATCCGACCGA SEQ ID NO:457 BM734722.V.3_at AATCAATACATTTTCCCGAGTCTGG SEQ ID NO:458 BM734722.V1.3_at TCGGCTGCCTGGTGMAGAGGTTCCT SEQ ID NO;459 BM734722MV.3 at GCGTTTCTGCAGCTATTTTTCTACT SEQ ID NO:460 BM734722.V.3_at GGTCCCGCGCATCAAAGACAAACTG SEQ ID NO:461 BM734722.V1.3_at GCGACTTCCAGTACGAGCTGGTCAT SEQ ID NO:462 BM734722.Vi.3_at GAAGAGGTTCCTCCGGAGACACAGT SEQ ID NO:463 BM734722.Vl.3_at GGAGACACAGTCTGTTCCAGCCGGT SEQ ID NO:464 BM734722.Vl.3_a t TGAAGTTTGGCCAAGAGGCTTCCCG SEQ ID NO:465 Triggering receptor expressed on myeloid cells 1, transcript variant 2 BM734862.V1.3 at, ATCTACATCCATCTGGCAGTTGTGC SEQ ID NO:466 BM734862.Vi.3_at ATGAGGATGACCTCTGATCTCCATC SEQ ID NO:467 BM734862.Vi.3_at -AGCATTGTCATTCCTGTGGCGTGCG SEQ ID NO:468 BM734862MV.3_at ACAAAGGTTATTTCTGAGGCTCAGG SEQ ID NO:469 BM734862.Vi.3_at CTCGTGACTAAGAGCCTGGTCCTTA SEQ ID NO:470 BM734862.V.3_at CCCTCATTTCACTGATGACCGTGGG SEQ ID NO:471 BM734862.V1.3_at GAAGTCATTTGGATCCTAGGCCCAT SEQ ID tNO:472 BM734862.Vi.3_at TGGCGTGCGCACTCGTGACTAAGAG SEQ Ib NO: 473. BM734862.V1.3 3_at GGCAGCGACATGAGTTGGATCCGT-T SEQ ID .NO:474 BM734862.V1.3_at TAAAAGAGCAGACACGGCCCCAAAC SEQ ID NO:475 BM734862.V.3_at TTACTGTCCTGTTTGCTGTCACACA SEQ ID NO:476 Nuclear receptor binding factor 1 BM734865.V.3_at ACCACAGTCCAGAGCAGTTCCAGGG SEQ ID NO:477 BM734865.V1.3_at AGGACTACCAGCGTGCCTTGGWAC SEQ ID NO:478 BM734865.VI.3_at AAGGCCAGAGGAGCCAGAGCCAAGT SEQ ID NO0:479 BM734865.V1.3 at CAAGCAGATTCTCACCATGGGATAA SEQ ID NO:480 BM734865.Vi.3_at GATCAGCAGGACTGGTTTCGGGCCC SEQ ID NO:481 BM734865.V1.3_at GAAACTGCGATGCAGCCCTTCGTGT SEQ ID NO:482 BM734865.V1.3 at GAAGCCAGCCAAGGCTTTTCCCAGG SEQ 165 NO:483 BM734865.V1.3_at GGCTTTTGGTTGTCCCAGTGGAAGA SEQ ID NO:484 BM734 865. Vi. 3at TGATCCTCACGCTGTGCGATCTCAT SEQ ID NO:485 BM734865.V1.3_at TCACTGTCACTTCCAACCAGAAGAA. SEQ ID NO:486 BM734865.Vl.3 at iTTCGTGTCTTCCAAGCAGATTCTCA ISEQ ID .NO:487 -350- Set Nane .PROB EUc .Z Sevue as Equus caballus lipopolysaccharide receptor (CD14) mRNA, member 6 variant BM734889.Vl.3_at AGGAATCCCTATCTGGACCCTGAAG SEQ ID 140:488 BM734889.V1.3_at AGCAAGACCAGAACTCCGGOGTGGT SEQ ID NO:489 BM734889.V1.3_at AGCGCACTGAGTTCTCTCAACTTGT SEQ ID 140:490 BM734889.V1.3_at AACAGGCTCAACAAGGCGCCGCGAG SEQ ID 140:491 BM734889.V1.3 at CAACTTGTCCTTCGCTGGGCTGGAG SEQ ID 1O;492 BM734889.V1.3 a t GCCTAAAGGACTACCGGGCAAGCTT SEQ ID 140:493 BM734889.Vl.3 at GCCTCATTAGGACGTCTTAACCAAC SEQ ID 140:494 BM734889.V1.3 at GCTGCCCGTGGTGAGTAATCTGATA SEQ ID 140:495 BM734889.Vl.3 at GAATTGACTCAGATTGCCCTGGCTC SEQ ID 140:496 BM734889.V1.3_at GACCCTGAAGCGTCCAAGCAGCAAG SEQ ID NO:497 BM734889.Vl.3_at TTAGCGTGCTTGATCTCAGCTGCAA SEQ ID 140:498 C0P9 constitutive photomorphogenic homolog subunit 7A ______________________ BM735102.Vl.3_at AGGAACAGGTGAGCCGTGCCAACCA SEQ ID NO.:499 BM735102.vl..3_at AACTGAAGGG3ACTGTCGTCTOTTTC SEQ ID NO:500 BM7351O2.Vl.3_at AATCAGCGGCTGGAGGTTGACTACA SEQ ID 14:501 BM735102.V1.3 at GCATAGATCACACCTTCTCTAGGGA SEQ ID 14:502 BM735102.V1.3_at GACTACAGCATTGGGCGGGACATCC SEQ ID NO: 503 BM735102.Vl.3 at GTTACAACAGCAGCAGCAGCCGCAG SEQ ID 140:50f4 BM735102.Vl.3 at GGACCCTGAdCAACACCTGACTGAG SEQ ID NO:505 BM735102.Vl.3 at TAATCCTAGGTTCATGACCCTTCAC. .SEQ ID 140:506 BM735102.V1.3 at TGAGGGAACCAGCTCCTGGCACTAA SEQ ID NO: 507 BM735102.Vl.3_at TGCCCGAACCCTGCAAGAGTGGTGT SEQ ID 140:508 BM735102.Vl.3 at TTTAGGAGTCCTCAGAGAGCCTTCC SEQ ID NO:509 No homology BM735166.v1 .3 at ATGGTCGCCAAOTGGAACGTCT GGT SEQ ID .1:510 BM735166.Vl.3_at AGGCAGGATGCCCAGTGGCCAATAC SEQ ID go-.511 BM735166.Vl.3_at AGGGCACCCAGCATGGTTGAGTCTG SEQ ID 140:512 BM735166.Vl .3._at AGTGdCAGGTTGCCTGTGGCATCCAT SEQ ID 140:51:3 BM735166.Vl.3 at AGCTCAGGGCCTTGTAGTGCAGGTT SEQ ID NO:514 BM735166.V1.3_at CATGTTTATTATTACCCCGTGGCGG SEQ ID NO:515 BM735166.Vl.3_at CTGTGGGTTCAGGTTCATGTTTATT SEQ ID 14:516 BM735166.Vl.3_at GAAGGCCTTCCTTGAAGGAGCCCAT SEQ ID 14:517 BM735166.Vl.3_at GGAGGAACCCACAGGCAGATGCTCA SEQ ID 140:518 BM735166.V1.3 at TGTGCGGACAAGCAGCCACTGATCA SEQ ID 14:519 BM735166.V1.3_at TCAACCTCTGCTGACCACTGAGTGA SEQ ID 140:520 TAM'E SEQ ID NO:521 BM735167.V1.3 at AGGCTCTGCAGGACTGGATATCCCG SEQ ID 140:522 BM735167.V1.3_at ATGGCTGTCTTCATGACCTGGAGTA SEQ ID 140:523 BM7 35167 .V . 3_at GCTCACAGGCTGCAGACGGTTCAGA BM735167.V1.3_at IGAACGGTGCTGGTGATCGCTCACAG SEQ ID 140:524 BM735167.V1.3_at IGATTTGGACCTTGTGTGCTTTCATT SEQ ID NO:52 5 -351- PRB-2'~iC seoence. ____________________________ I'dentifier BM735167.V1.3_at GTGTCCATGAACCTTATTTCCTTGA SEQ I D N0:526 BM735167.Vl.3_at GGAGTAGCTCCTGCTTTGAGTTTCC SEQ ID NO: 527 BM735167.V1.3_at TGGACGTCCAGTGTGAGCAGGCTCT SEQ I D NO:528 BM735167.V1.3 at' TGGATCATGCCCAGCTCATGGAGGG SEQ ID NO:529 BM735167.V1.3 at TGGATGAAGCCACCAGTGCCCTGGA SEQ I D NO:530 BM735167.V1.3_at TTCAGAACGCTGACCAGATCCTGGT SEQ I D NO:531 Ferritin light chain BM735286.V1.3_at AGGAGCCTCCGGAGTCCAGCGGCCT SQI O 3 BM7528.V.3 t GCTTTTACAGCTGAGCTTSEQ ID NO:532 BM735286.V1.3 at CAAGCTTACTGCCTGAGCCTT SEQ ID NO:534 BM735286.V1.3_at CTGCAGCCACTAGAGATAGCTTTTT SEQ ID NO:535 BM735286.Vl.3_at CTCCGGAGTCCAGCGGCCTTTGAGG SEQ ID NO: 536 BM735286.V1.3 at CTGGCGTCAGAGCTTCTGCCTGAGC SEQ ID NO: 537 BM735286.V.3_at GAGATAGCTTTTTMACTAGCCTGGA SEQ ID NO:538 BM735286.V1.3_at TTTGGTATCCCCCTGGCGTCAGAGC SEQ ID NO:539 BM735286.V1.3_at TCCCTGCAGGCACTAGAGATAGCTT SEQ ID NO:540 BM735286.V1.3 at TTTTAACTAGCCTGGAGCCTTCTGC SEQ ID NO:541 BM3586V13 tTAACTAGCCTGGAGCCTTCTGCCCA SEQ ID NO:542 BM735286.V1.3_s-at ATGAAAGCCGCCATTGTCCTGGAGA SEQ ID NO:543 BM735286.V1.3_s-at ATTGTCCTGGAGAAGAGCCTGAACC SEQ ID NO: 54*4 BM735286.Vl.3 s-at ATCCAGAGGCTCGTTGGCTCCCAAG SEQ ID NO:545 BM735286.V1.3_s-at ATCTCTGTGACTTCTTGGAGAGCCA SEQ ID NO:546 BM735286.Vl.3_s at GATGGGCGACCATCTGACCAACATC SEQ ID NO:547 BM735286.V1.3s s at GGGCTGGGCGAGTATCTCTTTGAAA SEQ ID NO:548 BM735286.V1.3_s at GGGTACAACCCTGGATGCCATGAAA SEQ ID NO:549 BM735286.V1.3_s-at TGGAGAGCCACTTCCTAGACGAGGA SEQ ID NO:550 BM735286.V1.3_s-at TCTTTGAAAGGCTCACCCTCAAGCA SEQ ID NO:551 BM735286.V1.3_s-at TGAACCAGGCCCTTTTGGATCTGCA SEQ ID NO:552 BM735286.V1.3_s-at TTGGATCTGCATGCCCTGGGTTCTG SEQ ID NO:553 No homology BM735352.V1.3_at ATCAGACTGCACTGCCTGCGGGAGG SEQ ID NO:554 BM735352.V1.3 at AGCAGTCAAACCAAAGCATTCCATT SEQ ID NO:555 BM735352.Vl.3_at GTTATGGCCTAATGCCCACTTTTGT SEQ ID NO:556 BM735352.Vl.3_at GACGGAGCAAGCTGTTGCCATCAGA SEQ ID NO-557 BM735352.V1.3_at GACCCAGGGAGAGAACGTCGCTGCT SEQ ID 90:558 BM735352.V1.3 at GTCTGTGTTCAAGTACCTCACGGGA -SEQ ID NO:559 BM735352.V1.3_at GTCGCTGCTGTATACTGTAACGTCT SEQ ID NO;560 BM735352.V1.3 at GGGACGCTCCAGATATTTGAATCTC SEQ ID NO:561 BM735352.Vl.3_at TGATCCTCCTCCTGCGCAGAATAGA SEQ ID NO:562 BM735352.V1.3_at TGCTCACACGTAACAGTCTGGTGGG SEQ ID NO:563 BM735352.V1.3_at TCTCTATTAACTTACTGCTCACACG SEQ ID NO:564 No homology BM735409.V.3_at ATCTTGCACCTTCTTCAGGATTTTA SEQ ID NO:565 BM735409.V1.3_at ACCTGCCTGGGCTTCTGGGCCTGTG SEQ ID NO:566 BM735409.V1.3_at ACAGAGGGAGCCAGCAGCTGTCCCC SEQ ID NO:567 BM735409.V1.3 at ACACACTTTGCGTATCTGAGCGCGC _ jSEQ ID NO:568 -352-- Sia . POB ISqueceNC I-PR BM735409.V1.3 at AAAGCAGTACCTGGTGGCCGTGTGC SEQ ID NO:569 BM735409.V1.3_at GAAGTCAGAAGCCAAGCTTTCTCCC SEQ ID NO:570 BM735409.V1.3_at GTACCTCCTCCTCTGGAGGTGCTGG SEQ ID NO:571 BM735409.V1.3_at GGAAGCGCTGGAGCCACCCCGTGAA SEQ ID 140:572 BM735409.V1.3_at TGGCCTGGGCTCTGTCTACAGCCAC SEQ ID 140:573 BM735409.V1.3 at TCGCACTGGGTCTTATCTTGCACCT SEQ ID NO:574 BM735409.V1.3_at TCTGTGGGCCGCACGTACACACACA SEQ ID 140:575 JKTBP1 (alternative splicing). ________________________ BM735419.V1.3_at ACCGAATCCAGGTGTGGCACGCGGA SEQ ID NO:576 BM735419.V1.3_at AGAAGGCGCCTGACTTCGTGTTCTA SEQ ID 40:577 BM735419.V1.3_at .ACGAGCTGTACATGCGCCGCAGGAA SEQ ID 140:578 BM735419.V.3_at AAAGATTGGCTTCCQGTGGAGTGAA SEQ ID 140:579 BM735419.Vl.3_at ACAAGTCTGGGTACCTAGGCTCTGA SEQ ID 14:580 BM735419.Vl.3_at AACAAGCGGATCCTGCAGCTGTGCA SEQ ID NO:581 BM735419.V1.3_at CTACGCTGTGCAGGCCAAGTTTGGA SEQ ID NO:582 BM735419.V.3_at GAACAGACCTTTGGCTTGGAGTCGA SEQ ID NO:583 BM735419.V1.3_at GATGCCCTTGGACTGAATATTTATG SEQ ID NO:584 BM735419.V1.3_at GTATCTGAAGATTGCCCAGGACC-TG SEQ ID 140:585 BM735419.V1.3 at TGTGCATGGGCAACCACGAGCTGTA SEQ ID 140:586 WD repeat domain 1 BM735441.Vl.3_at ATGATGGTGTACGTCTGGACCCTCA SEQ ID NO:587 BM735441.V1.3_at ATGGTCACCATGCAAAGATCGTCTG SEQ ID 140:588 BM735441.V1.3 at AGTGGTCACAGTCTTAAGCGTTGCT SEQ ID 140:589 BM735441.V1.3_at AGATQTGTACACGTCCTTCTGAAAG 'SEQ ID 140:590 BM735441.V1.3_at AGAACGCGGCGTTTCTCTAAATCCT SEQ ID 14:591 BM735441.Vl.3_at ACGGGCCGCATCAGGGACGAGATTC SEQ ID NO:592 BM735441.V1.3_at GACAACGAGCATTTTGCCTCTGGCG SEQ ID NO:593 BM735441.V1.3_at GTTGCTGACGGCTACTCGGAGAACA SEQ ID 140:594 BM735441.V1.3_at GTCAAGATCCAAGATGCACACCGCT SEQ ID 140:595 BM735441.V1.3_at TGGACGAGCACACGTTGGTCACGAC SEQ ID 14:596 BM735441.V1.3_at TCGTCTCTCTACAGGGTGTTCAGAT SEQ ID 140:597 Lymphocyte surface antigen precursor CD44_________________ BM735450.V1.3 at ATTCTCGCAGTTTGCATTGCTGTCA SEQ ID 140:598 BM735450.V1.3_at AGAGAAGACTCCCACTACCAAAGAC SEQ ID 140:599 BM735450.Vl.3 at AGAGCAGTCCCTGGGTG1'CTGACAG SEQ 1D N0:600 BM735450.V1.3_at AGAATGGCTGATCATCTTGGCGTCC SEQ ID 140:60. BM735450.V1.3_at ACCTGCACCTTGACCTTGGGAAGAA SEQ ID 140:602 BM735450.V1.3_at CGACGAGACACGGAACCTGCAGAAT SEQ ID 140:603 BM735450.Vl.3_at GACCAGTTTATGACAGCCGACGAGA- SEQ ID N0:604 BM735450.V1.3_at GACCAOCCACGGATCTGAAACAAGT SEQ ID NO:605 BM735450.V1.3_at GAGTCGTCAGAGACCCAAGACCAGT S4Q ID 14:606 BM735450.Vl.3_at GGGTCCCATACGGAGACCTCAAATT- SEQ ID 14:607 BM735450.V1.3 at TGTGATGTGCTACTGACTGCTTCAT ISEQ ID NO:608 Nlo homologyII BM735457.Vl.3 at JAGGAACCTAACCTGATGCTCTTTCG ISEQ ID 14:609 -353- PROBE q squnc - *. Identifier BM735457.V1.3 a t AGGACCCAACTCTGAATACATTTTT SEQ I D NO1:610 BM735457.V1.3_at AGGGCAGTTTTCTTTGCCCAAGCCT SEQ I D NO:611 BM735457.Vl.3 at AGCCTGCACATCTTCTCAGCAAAAA SEQ ID 1.1:612 BM735457.V1.3 at AAGCCTTCGGTGCTAGTTAGCTCTC SEQ ID NO:613 BM735457.V1.3_at AAOTCCCTTAATCTTTCACACATGC SEQ I D NO:614 BM735457.V1.3_at GCAATAATCCCCACCTGTCTAAAAA SEQ I D NO:615 BM735457..V1.3 at GAAGATTTCTCTCTGTGACTGCAAC SEQ I D NO: 616m BM735457.V1.3 at GAGAGGTTGCCCTACGAACAGACAG SEQ ID NO:617 BM735457.V1.3_at GAAATGTTAACTCCCTTTTGCAGAA SEQ ID NO: 618 BM735457.V1.3 at GATTGAGATTCAACCTGGCCTTACC SEQ ID NO: 619 No Homology BM735487.V1.3_at GAGTTCGAAGTCACCCTAATCACGT SEQ ID NO: 620 BM735487.V1.3 at CACCAGGACTCTAGCCCCAGAGTGG SEQ ID NO: 621 BM735487.V1.3_at AAATGGA.ACTCTCCTTTTCGAGCAT SEQ ID NO:622 BM735487.V1.3_at CGGCCCGGACACAAGGAGGAAGCTC SEQ ID NO: 623 BM735487.V1.3_at GCGTCTGACCCCAGCGAAGGGCCAG SEQ ID 1.1:624 BM735487 .V1. 3_at GAAGGGCCAGCCTTGCTTGGTTCAG SEQ ID NO: 625 BM735487 .V1 .3 at GACTGTGGAGGGACAGGCTTCCCCT SEQ ID NO:626 BM73-5487.V1.3_at GTTAGCTTOCCCCAAGAATTGTGT SEQ ID NO: 627 BM735487.V1.3_at GTCACOCTAATCACGTAAATGGAAC SEQ ID NO: 628 BM735487.V1.3_at GTGCTTGCTTGGGAGTTCGAAGTCA SEQ ID* NO: 629 BM735487.V1.3_at 'TAGCCCCAGAGTGGCTCCAGAAGGT- SEQ I D NO: 630 Ring finger protein 10, clone ERLTF2001835 BM735519.V1.3_at CAGGCTACCTTCTCCATTTGGt~TTT SEQ I D NO: 631 BM735519.V1.3 at AGATGTGTGGCCCAAAACTGCTCCA SEQ ID NO: 632 BM735519.V1.3 at AGCCT TCATGAAGCTGGACACGCCA SEQ ID NO:633 BM735519.V1.3 at AGAAGCTCCTGTTCAGCACCTCAGT SEQ ID NO: 634 BM735519..V1.3_at AATACAGTGTATT.TTCCAGCTTCCT SEQ ID NO:635 BM735519.V1.3 at CAAGTGACACTACTGGCCCAGGCTA SEQ ID NO: 636 BM735519.V1.3 at CCGTGCTTTTGTTTTGCTGCTGTAA SEQ ID NO: 637 BM735519.V1.3_at TGAAAACAGCTTAATTCCTCCYGQC SEQ ID NO:638 BM735519.V1.3_at TGATAACTCGGACCGTGTTCCTGTG -SEQ ID Nd:639 BM735519.V1.3 at TTCCAGAATTCCTTCAGCCAAGCTA SEQ I D NO:640 BM7.35519.V1.3_at TTCGGATCCCCTCTCTGAAGAGAAA SEQ ID NO:641 PREDICTED: Boa taurus similar to hypothetical protein (L0C515494)_________________ BM735534.V1.3 at ATTAGAGGGCAGCTCAGCCTCCCTT SEQ ID NO:642 BM735534.V1.3_at AGGATCATAGGCCTGGACACTCCAT SQID NO:643 BM735534.V1.3 -at AGTCACAGTGACAACAACCCATTAG SEQ ID NO:644 BM735534.V1.3 at AGAGGATGAGCCACTGCTTGCCTGA -SEQ ID NO:645 BM735534.V1.3_at -ACTGCTTGCCTGAGGTGACCTGGCT SEQ ID NO:646 BM735534.V1.3_at AATGCCAATTGGCTGGAGACTTCCA SEQ ID NO:647 BM735534.V1.3_at AATGCCATAGGTTAGATGTCCCTCA SEQ ID NO:648 -354- PROBE SEQU -ik~eE ~zcDBEsequence*., BM735534.V1.3 at CACCATTCAGGTGGCTGTTTTTAAA SEQ ID NO:649 BM735534.V1.3_at GCATTTGGGCAGAGCCTGAACTCAA SEQ ID NO:650 BM735534.Vl.3 at GAGAGAGGGCTCACACAGAGCTCCC SEQ ID NO:651 BM735534.V1.3_at TATCCCATAGCTAGGTTATTGCCCA SEQ ID NO:652 Transglutaminase E3 (TGASE3) (6 sialyltransferase), transcript variant 2 BM735536.V1.3 at GTCCCGGGTAQGTTTTGAGATCCTG SEQ ID NO: 653 BM735536.V1.3_at ACAAGTTCCCTGCAATCAAGGCCAT SEQ ID NO:654 BM735536.V1.3_at ATGCTGTCCATCGACGTGGCTGAGT SEQ ID NO:655 BM735536.V1. 3_at AGTCGGTCTGGACTGTTTGCTGATC SEQ ID NO:656 BM73!5536.Vl.3_at AGCGACCCTCCGAATGGATGCTCAG SEQ ID NO:657 BM735536.VJ..3_at ACGCCCATCAATGCTGCAGGACAGA SEQ ID NO:658 BM735536.V1.3_at GACAGAGTGGCACCTGACCCAGCGA SEQ ID NO: 659 BM735536.V1.3_at GACTTGATCACTTTTGCACATTCCC SEQ ID NO:660 BM735536.V1.3 at GGTTAACCATCTGTCATGGCACTCG SEQ ID NO:661 BM735536.V1.3 at TGCAGTTGGGACATTCGTGCTACTC SEQ ID NO:662 BM735536.V1.3 at TTGCTGACTTCTCCTGCGACAAGTT SEQ ID NO:663 CD68 protein BM735545.V1.3_at ACAGGAGCCTTTGGGCCAAGTTTCT SEQ ID NO:664 BM735545.V1.3_at ATTACCTTCTGTGTCATCCGGAGAC SEQ ID NO:665 BM735545.Vl.3_at AGAGACCAAATTATCtTCdTTCCCT SEQ ID NO:666 BM735545.Vl.3 at AGAAACGCAAGCATCGCTCTTTCAC SEQ ID NO:667 BM735545.V1.3_at AAATCTTTGTCCCTGATTTCCCTTG SEQ ID NO:668 BM735545.V1.3 at AAGTTTCTCTTGTCCCAGTGACCAG SEQ ID NO:669 BM735545.V1. 3 at CTGAAGCTACAAGCTGCTCAGCTGA SEQ ID NO: 670 BM735545.V1.3 at CCTAGGCCAGAGATTCAGTTGCAGA SEQ ID NO: 671 BM735545.V1.3_at TACTCGGCCGACTCAGAGACCAAAT SEQ ID NO:672 BM735545.V1.3_at TACCAGCCACTCTGAGCGTTTATCC SEQ ID NO: 673 BM735545.Vl.3_at TTCCCTCTCTGTCCTGAAGAACAAA SEQ ID NO:674 No Homology BM735573.V.3_at ACTAGTGTGGGAGAAACCAGCTTTT SEQ ID NO:675' BM735573.Vl.3_at ATCACTGCTTTACTCTGTTAATTTA SEQ ID NO:676 BM735573.V1.3 at AAAAATCACTGCTTTACTCTGTTAA SEQ ID NO: 677 BM735573.V1.3 at AAATCACTGCTTTACTCTGTTAATT SEQ ID NO:678 BM735573.V1.3_at CACTGCTTTACTCTGTTAATTTACA SEQ ID NO:679 BM735573.V1.3 at GCTTTTACTGTTTAAAAATCACTGC SEQ ID NO:680 BM735573.V1.3 at GCTTTACTCTGTTAATTTACAAGGA SEQ ID NO: 681 BM735-573.V1.3_at GApATTCGGCACGAGGAAATTCCTAA SEQ ID NO: 682 BM735573.V1.3_at GATACTACAGTGAAACTAGTGTGGG SEQ ID NO: 683 BM735573.V1.3_at TGGGAGAAACCAGCTTTTACTGTTT SEQ ID NO: 684 BM735573.V1.3_at TCGGCACGAGGAAATTCCTAACAAG SEQ ID NO: 685 Minor histocompatibility antigen H13 isoform 1 (H13), desmosome associated protein _________________ -355- Prbe'q Sbt d - PRO3 -SQ~c Y~ seene (PNN)__ _ _ _ _ _ _ _ _ _ _ _ _ _ _ _ BM735576.Vl.3_at ATCTTCATCATGCACATCTTCAAGC SEQ ID NO: 686 BM735576.Vl.3_at AGGGATGGACCAGCACAGGCCTGCA SEQ ID NO: 687 BM735576.Vl.3_at CATCCTGGTGGCACTGGCCAAAGGA SEQ ID NO:688 BM735576.Vl.3 at GCATGTGGCAGGATCCCTCCAGCAG SEQ ID NO:689 BM735576.Vl.3 at GAAATGATGCGGCTGCtGCCTGACC SEQ ID NO: 690 BM735576.V1.3_at GAGTCAAGCCCTAAGGATCCAGCGG SEQ ID NO:691 BM735576.Vl.3_at GATCCAGCGGCAGTGACAGAATCCA SEQ ID NO:692 BM735576.V1.3_at GGGAACAGAGGCCTCAGCATCAAAG SEQ ID NO: 693 BM735576.V1.3_at TGCGGTTTGACATCAGCTTGAAGAA SEQ ID NO: 694 BM735576.Vl.3_at TGGGTCTTACCATCTTCATCATGCA SEQ ID NO: 695 BM73557 6.Vl1.3_at TTGAAGAAGAACACCCACACCTACT .SEQ ID NO: 69.6 Pc-epsilon-receptor gammia- chain______________________ BM735585.Vl.3_at ATGATTCCAGCAGTGGTCTTGCTCT SEQ ID NO:697 BM735585.V1.3_at ACCCTACCCCTGTAATGATGCTATG SEQ ID NO:698 BM735585.Vl.3_at CTGCCATTAATGCTAGCTGACCCTA SEQ ID NO: 699 BM735585.V1'.3-at GTACCCGGACCCAGGAGACTTATGA SEQ ID NO:700 BM735585.V1.3 3at GAGAGCCTCAGCTTTGC.TATATTCT SEQ ID -NO: 701. BM735585.V1.3 at GATGCCATCCTGTTCTTGTATGGTA SEQ ID NO:702 BM735585.Vl.3_at TGTTTATAT.TCTAGTCTCACCCCTA SEQ ID NO:703 BM735585.V1.3_at TTTCAAACAGATGCCCTTGGTCACA SEQ ID NO:704 BM735585.Vl.3_at TAACGGACATCAGTGGTTCCTCTTC SEQ ID NO:7 05 BM735585.Vl.3 at TTGGTTGAACAAGCAGCGGCCCTGG SEQ ID NO:706 BM735585.V1.3_at TTGCTCTTACTCCTTTTGGTTGAAC SEQ ID NO:70 7 BM781012..Vl.3 at CAGAAGAACGTCTCCAAGAACCCGG SEQ ID NO:708 BM781012.Vl.3 at CACCAAGACCAAAGGGCGGTCCCAG SEQ ID NO:709 BM781012.Vl.3 at AGGAGCCGCAAGTGTACGTCCTGGC SEQ ID NO:710 BM781012.Vl.3_at AGTTCAACAGCACTTACCGCGTGGT SEQ ID NO:711 BM781012.Vl.3 at AATCAACATOGAGTGGCAGAGTAAT SEQ ID NO;712 BM781012.Vl.3_at ACCCAGACGAGCTGTCCAAGAGCAA SEQ ID NO:713 BM781012.V1.3_at ACGAGCTGTCCAAGAGCAAGGTCAG SEQ ID NO: 7 14 BM781012.V1.3_at AAGCTCTCCGTGGACAGGAACAGGT SEQ ID NO:715 BM781012.Vl.3_at GCACTTACCGCGTGGTCAGCGTCCT SEQ ID NO:716 BM781012.Vl.3_at TCGAGAGGACCATCACCAAGACCAA SEQ ID NO:717 BM781012.V1.3_at TACCCACCTGAAATCAACATCGAGT SEQ ID NO:718 GM2 ganglioside activator BM781174.V1.3 at AGCTGGCTCAGCAACGGGAACTACC SEQ ID NO:719 BM781174.V1.3 at AACGCTGTCACAGACCTAGCAGTTA SEQ ID NO:720 BM781174.V1.3_at AAGTGGCTGGCGTATGGGTCAAAAT SEQ ID NO: 721 BM781174.V1.3 at GCGGACCCACCATTTGCAATGAGAC SEQ ID NO:722 BM781174.V1.3_at GCTGTACTTTTGACAATGCCTGTGA SEQ ID NO:723 BM781174.V1.3_at TAGCAGTTAACCAGGCGCGGACCCA SEQ ID NO:724 BHM781174.Vl.3_at GAACTACCGTGTCCAGAGCATCCTG SEQ ID NO: 75 BM781174.V.3_at GGGAAGGACCCTATGGTGCTCAAAA ISEQ ID NO:726 -356- Rxobe, Set:,.~ RBE sqece *" PR B9, S BM781174.V1.3_at GGCTCCGTAGCTTTTCCTGGGATAA SEQ ID NO:727 BM781174.V1.3_at TGGTGCTCAAAAGCCTGACTCTGGA SEQ ID NO:728 BM781174.V1.3_at TGATATACTAGACGCTTTGACTCCC SEQ ID NO:729 No homology BM781178_unkn.V1.3_at ATAGCCTCCATTTCCTTCAATAGAT SEQ ID NO:730 BM781178_unkn.V1.3 at ATCGTTTAAGGCAGATGTCCCCGGA SEQ ID NO:731 BM781178_unkn.V1.3_at ATCACCAGTTCTTATGTCACCTTAG SEQ ID NO:732 BM781178 unkn.V1.3_at AGTGGGATGCCTTAAACACCCGCAC SEQ ID No:733 BM781178_unkn.V1.3_at CAACTGGTATCTGTCATCTGGTAA SEQ ID NO:734 BM7.81178_unkn.V1.3 at GCAGACCGATGTGGTACCGGCTGAA SEQ ID NO:735 BM781178_unkn.V1.3 at GATGTCCCCGGAAGAGCAGTTTTTT SEQ ID NO:736 BM781178_unkn.V1.3_at GGGATGCCTCAAAATGCAGACCGAT SEQ ID NO:737 BM781178_unkn.V1.3_at GGATCCGATCTATTGTTACAGGCAC SEQ ID NO:738 BM781178_unkn.V1.3 at TGGTTCGTTATCTTCTCTTTGGCAA SEQ ID NO:739 BM781178_unkn.V1.3_at TGGGTTGCTACTGCCATGGTTTGAA SEQ ID NO:740 BM781178.V1.3_at ATTTTGAGGCATCCCTTCTAGGTGC SEQ ID NO:741 BM781178.V1.3_at AAATGGAGGCTATCGTCATGGCAGG SEQ ID NO:742 BM781178.V1.3_at CAGTTCCTTCAAACCATGGCAGTAG SEQ ID NO:743 BM781178.V1.3_at GATCCCCTCTGGTTATAGTTCGTGA SEQ ID NO:244 . BM781178.V1.3 at GTAGCAACCCAGTGCCTGTAACAAT SEQ ID No:745 BM781178.V1.3_at GGGAATATTCTTTCAGCCGGTACCA SEQ ID NO:746 BM781178.V1.3_at TTTAAGGCATCCCACTGTAGACTCT SEQ ID NO:747 BM781178.Vl.3_at TGTAGACTCTTCTCTCGGGAATATT SEQ ID NO:748 BM781178.V1.3_at TCTGTCCCCACCATTGATTCTAAGG SEQ ID NO:749 BM781178.Vl.3_a.t TACCACATCGGTCTGCATTTTG.AGG SEQ ID NO:750 BM781178.V1.3 at TAGGTGCTCAATGCCATTACCAGAT SEQ ID NO:751 Membrane-spanning 4 domains, subfamily A, member 6A, transcript variant 1 BM78'1186.V1.3_at ATAGGAGCCTTGTGTTTTGTGATCT SEQ ID NO:752 BM781186.V1.3_at AAGCCTTTGGTTCAGAGCAGCCTAG SEQ ID NO:753 BM781186.V1.3 at AAGT-TCTCGGGACTATCCAGATCCT SEQ ID NO:754 BM781186.V1.3_at CAGCATTTTACCCAAGCGTTtTCTA SEQ ID NO:755 BM781186.V1.3 at CTGCAAACATTCTGAGCTCTCTATC SEQ ID NO':756 BM'781186.V1.3_at GAAGGCTGCTTACCCATTCATAGGA SEQ ID NO:757 bM781186.V1.3_at GAATTATTTTGGCATCGGCTTCCTT' .SEQ ID NO:758 BM781186.V1.3_at GTCATACTGGCTTCTTTGGGTCCTG -SEQ ID NO:759 BM781186.V1.3_at GTCATCTCTGGATCTCTATCAATCA SEQ ID NO:760 BM781186.V1.3_at TAGCTGGAACCAACGGGCTGATCCT SEQ ID NO:761 BM781186.V1.3_at TATCAGCTCTGGTGGGTTTCATCCT SEQ ID NO:762 No homology BM781334.Vl.3_at GTCAAGTCTGACTGAATGAGGCCAC SEQ ID NO:763 BM781334.V1.3_at AGAGGGACCTCGTCAGGCACTTCtA SEQ ID NO:764 BM781334.V1.3_at ACTGCAGTAGTGACCCTTCAAGAGG SEQ ID NO:765 BM781334.Vl.3_at AAGAGACGTCATGGCCCCGTACGTG SEQ ID NO:766 8M781334.Vl.3_at CAGCCACTGGCTGATTTCAAGTCAT SEQ ID NO:767 -357- 7k ... Sequence - - .. "{, ** . . .Identi.fi r BM781334.V1.3_at CTGGTGGAAGAGATCCCGCGGAACC SEQ ID 140:768 BM781334.V1.3_at GCCCTCGGAGCTTCTGCTGGTGGAA SEQ ID 140:769 BM781334.V1.3 at GAAGCCCCTAGCTCAGGCAGAACAG SEQ ID 140:770 BM781334.V1.3 at TGGAAAGTCCAGAGGTGTCACCAGG SEQ ID 140:771 BM781334.V1.3_at TGGCTGTGATTGGAGTTCCGGACAT SEQ ID 140:772 BM78.1334.V.3_at TGTCCCACAGGGAGCTCA&AGAGTG SEQ ID NO:773 No homology BM781417 .V1.3_at ATTTAGCTACTTTATTGCCTTTACA SEQ ID NO: 774 BM7.81417.Vi. 3_at A ATTGTTATTATTACGCTCTTTGCG, SEQ ID 140:775 BM781417.Vl.3 at GCCTTTACATTGOTTATTCTTATT'G SEQ ID NO: 776 BM781417.VI.3_at GCACTTTCTTTGATTACACTTCCAT SEQ ID NO: 777 BM781417.V1.3_at GAATTCTGTCCTTCATTTACTTTGT SEQ ID NO:778 BM781417.V1.3_at GAAAAGTCGTCTCCTAGTAACCAGT SEQ ID 140:779 BM781417.V1.3_at OACAAACAGCTTTAAGTGCACTTTC SEQ ID 140:780 BM781417.V1.3_at GATCTAGCTGGGAAACTGTCATGAG SEQ ID NO:781 BM781417.V1.3_at GTTGCTTTTTCCTTCTTTGATCTAA SEQ ID NO: 782 BM781417.V1.3_at TAACTTCAATCCTCAGATCTAGCTG * SEQ ID NO:783 BM781417.V1.3_at TTCTGAAGCCTTtTATGTACCACTA SEQ ID N .0:784 Homo sapiens 15 kDa selenoprotein, transcript variant 1 ________________ FoelO6O.Vl.3_at ATTTGCATTCTCCTACATTTGTTGA SEQ ID N0:785 FoelQ6O.Vl.3_at AGATATTCTAGCCTCCACAGATTGC SEQ ID 140:786 FoelO6O.V1.3_at AGATGATTGCTATGCTTCCTGTGCT SEQ ID 140:787 FoelO6O.Vl.3_at ACCTTTCTGAGGATTTGTGIGGATC SEQ ID 140:788 Foe1O6O.V1.3-at CCTCCAATCCGCTCATATTTTTGTA SEQ ID 140:789 YFoelO6O. V1.3 at GAAACATTCACAAAGATTCGCGTTA SEQ ID 140:790 FoelO6O.V1.3_at GTTGGCAAGCTTAACAAACCTGTTT SEQ ID NO:791 FoeiO6O.Vi.3_at GTGTGGATCTGATATCCGGCAAATT SQID 140:792 FoelO60.V1.3_at GGCAAATTTTTGTGCTTTACATTCT SE9Q lb 140:793 FoelO.Vl.3_at TGTATTACCCAGCTTTCCTTTAAAT SEQ ID 140:794 Foe1O6O.V1.3_at TGTGCTGTG TGCTCCTTGAAAGTAA SEQ ID 140:795 Transducii (beta) -like iX-linked receptor 1 FoelO72.V1.3_at ATAGATGTTCTATGCTGTCCTGGAC SEQ ID 140:796 FoelO72.V1.3_at ACATCACAATGATTTGTCCCCI GCG SEQ ID 140:797 FoelO72.Vl.3-at AACCAGCCCATGACAGTTTTTTGTA SEQ ID 140:798 FoelO72.V1.3_at GCAGTTTCCCTTTGCATTGTATTGC SEQ ID 140:799 FoelO72.V1.3_at GACCCTTTTATCCTTTCTAGGCACA SEQ ID 140:800 FoelO72.V1.3_at GACTGCATTTTGTAGCTCTGTAATC SEQ ID 140:801 FoelO72.Vl.3_at GTAATTTTCTTCTTTCCTGACTTTG SEQ ID 140:802 Foe1O72.V1.3_at * GTGAGCCTACCTATAG CACTGGATT SEQ ID 140:803 Toel072MV.3_at TGTCTGCATCATTTCTTTAGTTATC SEQ ID 140:804 Foel072.Vl.3_at TTTGGGTCTAATTCTGTGAGCCTAC SEQ ID 140:805 FoelO72.Vl.3.at TTCTGCATGTTGTATCTAGTCTGAT SEQ ID 140:806 Homo sapiens mRNA; cDNA DKFZp666Il86 ________________ -358- Prob6e..S x.ane... PROBE - sOflCEbq: .* *.. - .- .,,J$A.;.r1*9 .dntifi6r7 (from clone DKFZp666I186)_________________ Foe545.Vl.3_at ATGTGATAACAGOACCTCTTCATCT SEQ ID NO;807 Foe545.V1.3 at ACTTCAAGTCTTGCAATGGTGCTTT SEQ I D NO:808 Foe545.V1.3_at AAACGCAACCAGTTCATCGGGATTT SEQ I D NQ:B09 Foe545.V1.3_at CTTCCAAATTGGCTTTTACAGATCC SEQ I D NO:810 Foe545. V1.3_at CAGCACCTCTTCATCTTTAACTTGA SEQ I D NO:811 Foe545.V1.3_at CTTGGTTAGGAGTGGTTTGCTGCCC SEQ I D *NO: 812 Foe545.V1.3_at GAAATTTCCTTTTCTGAGTGTTGAA SEQ ID NO:813 Foe545.V1.3_at GTTAGCAGACTAGAAGACTTCCAAA SEQ ID NO:814 Foe545.V1.3_at GGAACATTTTACACACTTCAAGTCT SEQ ID NO:815 Foe545.V1.3_at TTTGCTGCCCTCCTCTAAAGGCAGT SEQ ID NO:816 Foe545.V1.3_at TTCCTGTOAGTTTCATCCAATCTTA SEQ ID NO:817 Foel0l9.V1.3_at AAAGTGCTACACTCCTTTGGTGAGG SEQ ID NO:818 Foel0l9.V1.3_at AACGTGCTGGTTGTTGTGCTGGCTC SEQ ID NO:819 Foel0l9.V1.3_at AAGAGAAGGCAGCTGTCTTGGCCCT SEQ ID NO:820 Foel0l9.V1.3_at TGGCAAGGATTTCACCCCAGAGTTG SEQ ID NO:.821 Foe1019.V1.3_at CAGAGTTGCAGGCTTCCTATCAAAA SEQ ID NO:822 Foe10l9.Vl.3_at GACAAGCTGCACGTGGATCCTGAGA SEQ ID NO:823 Foel0l9.V1.3 at GAGAAAGGCCTCTTTGTGCCCAAAG SEQ ID NO:824 Foe10l9MV.3_at GAGATCCTGGCTTCTGCCTAATAAA SEQ ID NO:825 Foel019.V1.3 at GATCTGTCCAATCCTGGTGCTGTGA SEQ ID NO:826 Foe1019.V1.3 at TGGTTGTCTACCCATGGACTCAGAG SEQ ID NO:827 Foe1019.V1.3_at TGAGGGCGTGCATCATCTTGACAAC SEQ ID NO:828 Equus caballus gelsoliri mRNA_________________________ GI1592834.V1.3_at ATCACCGTCGTGAAGCAAGGCTTTG SEQ ID NO;829 G11592834.V1.3_at AAAGACGGAAGCCTTGACCTCTGCT SEQ ID NO:830 G11592834.V1.3_at AACGATGCCTTTGTCCTGAAAACTC ' SEQ ID NQ:831 GI1592834.V1.3_at AAGGCAGCGAGCCAGACAGCTTCTG SEQ ID NO0:832 GI1592834.V1.3_at GAAGAGCTGGCCACTGATGACGTCA SEQ ID NO:833 G11592834 .V1.3_at GAAGAGGTCCCTGGCGAGTTCATGC SEQ'ID NO:834 GIJ592834.Vl:3_at GACCAGGTCTTTGTCTGGGTCGGAA *SEQ ID NO:835 GI1592834.Vl.3_at GACAGCTACTGGTCTGTGGATCCCT SEQ ID NO:836 G11592834.V1.3_at GTATATCGACACAGACCCAGCTCAT SEQ ID NO:837 G11592834.V1.3_at GGAGCCACCCGAGCCGTTGAGATAA SEQ ID NO:838 G11592834.Vl.3_at TCTTTGCCTGCTCCAACAAGATTGG SEQ ID NO:839 gi5441616.V1.

3 at ATAGCCTCACTAGAGGTCTAGCGGT SEQ ID NO:840 gi5441616.V1.

3 at AAACGTCTACTCTCTCCTGTAAGAA SEQ ID NO:841 g-i544161 6 .V1.3 at GCACCCCAGACCGTATTTATCATAT SEQ ID NO: 842 gi5441616.V1. 3 at GAATCAGATTACTTTGGCAGGCTTG SEQ ID 14:843 gi5441616.V1.3 at GACAACACACTTTACTTTGTAGCTG SEQ IDl 1:844 g15441616.Vl.3-at GACCAAGTTCTCTTCATTAACCAGG SEQ ID 14:845 gi5441616.Vl.3_at GGCAGGCTTGAACCTAAACTCTCAA SEQ ID 14:846 g15441616.V1.3.at IGGATATGCCTGATTCTGATTGTACA ISEQ ID 14:847 -359q;JU~~ 'm ... 'POESQUFNCE'I e.... gi5441616.V1.

3 at GGAAATGAGTCCTCCTGAGAATATC SEQ ID NO:848 gi5441616.V1.3 at TGATTGTACAGACAACGCACCCCAG SEQ ID NO:849 gi5441616.V1.3 at TAGCGGTAACCATCTCTGTGAAGTG SEQ ID NO:850 Equus caballus..Ig epsilon heavy chain (partial) _______ gi5766t26.V1.3 s-at TTAAGCCTGAACTGGTCCCGGGAGA SEQ ID NO:851 gi576646.Vl.3_s at AGAGCTCCAAGGACAAGGTCACCCT SEQ ID NO:852 gi576646.V1.3_s at AGACCCTGGTAAATGATGCCCTCTG SEQ ID NO:853 gi576646.V.3 s at AATTTGCCTGCAAGGTGGTCCACGA SEQ IQ NO:854 gi576646.V1.3 s at GAGACTTACAAGTGCACCGTGTCCC SEQ ID NO.: 855 gi576646.V1.3_s at GAAAGAGGTGTCCAAAGACCCTGGT SEQ ID NO:856 gi576646.V1.3 s at TGTCCCAAAGGACCCTCCAGAAAGA SEQ ID NO:857 g1576646.Vl.3_-s -at GTGGACACCACCGACTGGATCGAGG SEQ ID NO:858 gi576646.V.3_s-at GGGAGCCCCTGCAGAAGCACACACT SEQ ID NO:859 gi576646.V1.3_s-at TGCCCAGGGAAGTCGTGCGCTCCAT SEQ ID NO:860 gi576646.V1.3_s at TAATCCAGACAGACCAGCAAGCCAC SEQ ID NO:861 Equus caballus Toll like receptor 4 mRNA _______________ G19717252-3_at ATCTTTGACATCTTAGCCATCCTAA SEQ IQ NO:862 G19717252-3_-at AGAAGGCTCCTGATTCAGATCCTCC SEQ ID NO:863 G19717252-3_at ACATCGTCTCCCAAGTCTTTTGAAT SEQ ID NO:864 G19717252-3 at ACAGGACTGCTAATCCCTTTGAGTT SEQ ID NO:865 G19717252-3_at AAACATCCTGGTCATTCTTTAGCGT SEQ ID NO:866 G197.17252-3 at AAGTCAGCTAAGGAGTCCGTGCCAG SEQ ID NO:867 G197.17252-3_at GCTGCAACATACCAGGCATTGTGCT SEQ ID NO:868 G19717252-3_at GAATGGAAACCATCTC.ATCTTTGAC SEQ ID NO:869 G19717252-3_at GACTGGGCCCCAGTGAGTTCAGAAA SEQ ID NO:870 G19717252-3_at GGCAGGTGATTCTGTCGTGCACAAG SEQ ID NO:871 G19717252-3 at TCTCTGTTCAATTTTCCCTTTTCTA -SEQ ID NO: 872 G19717M5-3M at ATAAGTTCTATTTCOACCTGATGCT SEQ ID NO;873 G19717252-3Mat AGAGACTTCATTCCTGGTGTGGCCA SEQ ID NO:874 .G19717252-3M-at AAAGTTATTGTCGTGGTGTCCCAGC * SEQ ID NO:875 G19717252-3M at CAGCACTTCATTCAGAGCCGATGGT SEQ ID NO: 876 G19717252-3M at GCGGGTCGGTTTTCAGTATACTCAT SEQ ID NO: 877 G19717252-3Mat CTGATGCTTCTTGCTGGCTGCAAAA SEQ ID NO: 878 G19717252-3Mat GCATGCCCGTGCTGGGTTTTAACAA SEQ ID NO:879 G19717252-3Mat GATGCCTTTGTTATCTACTCAAGCC SEQ ID NO:880 G19717252-3M-at GGTGTGTGCAATACCCTTACAGATG SEQ ID NO:881 G19717252-3M .at TGAGTATGAGATTGCCCAGACCTGG SEQ ID NO: 882 G19717252-3Mat TTAACAATGCCACCTGTCAGATTAG SEQ ID NO:883 G19717252-5_at AGTTAGGCAGCCATAGCTTCTCCAA SEQ ID NO: 884 G19717252-5.at AGAAGTTCCCCATTGGACATCTCAA SEQ ID NO: 885 G19717252-5_at CATCTCTCCACCTTGATATTGACAG SEQ ID NO:886 G19717252-5_at GAAAATGCCAGGATGATGCCGCCCA SEQ ID NO:887 G19,717252-5_at GACCTGAATCTCTACAAAATCCCTG SEQ ID NO:888 G19717252-5 at IGTGCAGGTGGTTCCTAACACTACTT -SEQ ID NO: 889 -360- Pr o-biet lName '* eqluence G19717252-5_at GTGGCCGTGGAGACAAAGCTTTCAT SEQ ID NO: 890 G19717252r5 at TGGACTCTCCAGTTTACAGACGCTG SEQ ID NO:89. G19717252-5_at TGGACCTGAGCTTTAACCCCTTGAA SEQ ID NO:892 GI9717252-5_at TGATGCATATCAGGGCCTCAACCAT SEQ ID NO:893 G19717252-5_at TTACGGTGCGTCATGCTTTCACAGG SEQ ID NO:894 G197172K2-5M-at AAACAGGCCAGTGATTTTCCAGTAT SEQ ID NO:895 G19717252-5Mat AAAGATTTGACACATCTGCCCTGCG SEQ ID NO:896 G19717252-5M at GATATTTCTTACACTAACACCCGAG SEQ ID NO:897 G19717252-5Mat GCGCGGACTGCACAATTTGACGATT SEQ ID NO:898 G19717252-5Mat GAATTCCGGTTAGCATACATTGATA SEQ ID N'O:899 G19717252-5Mat GAAGGATTTCCCACATTGGAGCTCA SEQ ID NO:900 G19717252-5M at GATTTTCCAGTATTCTTATCCCTCA SEQ ID NO:901 G19717252-5M at GGATTTCCAGCATTCCACTTTGAAA SEQ ID NO: 902 GI19717252-5M at GGAGCTCACCTCTCTCAAAAGGTTG SEQ ID NO: 903 G19717252-5Mat TGAGTTTCAAGTCCTGCTGTTCTGA SEQ ID NO: 904 G19711252-5Mat TACCAAGCCTTGAGTTTCTAGATCT SEQ ID NO:905 No Homology________________________ WBC001AO7_Vl.3_at ATGGTGCCATGGCTGGTAGCTTTTA SEQ ID NO:906 WBCOO1AO7 V1.3_at AGGCAGACACTGCTGTATTTAGAAA SEQ ID NO:907 WBCOOlAO7_V1.3_at AAAACAGAACTCACAGCCTTTCTCC SEQ ID NO: 908 WBC001AO7_Vl.3_at GCTAATGAAGCTTCTCATOTTCTAT SEQ ID NO:909 WBC001AO7_Vl.3_at GAATATCTTGGCACACTTTAATGTC SEQ ID NO:910 WBC001A07_Vl.3_at GATATTTGTTGCACAGGCAGACACT SEQ ID NO:911 WBC001AO7_Vl.3_at GTAGCTTTTAGTGAGTGCTGCAAGA SEQ ID NO: 912 WBC001AO7_Vl.3_at GATTTTTCATCTGATTTGTTCACGC SEQ ID NO:913 WBCOO1AO7_V1.3 at GTTCACGCAAATGTAGTTCTTATCA SEQ ID NO: 914 WBC001AO7_Vl.3_at TATACAAAATTTCCATTCCTCCCAA SEQ ID NO: 91*5 WBC001AO7_Vl.3_at TTCTCCCTGTGTCTTTGGCAATGTA SEQ ID NO:916 WECO0lBIlV1.3_at ATGAGCGTCTTTTCTCAGTACTCAG SEQ ID-NO:917 WBCOO1B11_V1.3_at AAAATAGCACCTCTGTGTCTTCTCT SEQ ID NO:918 WBCOO1BlV1.3_at AACACAGCTGTCTCGATTTCTGGTG SEQ ID NO:919 WBCOO1B11_V1.3_at AAGGATGCATACTCAACCTCTGATC SEQ ID NO: 920 WBCOO1Bl1_Vl.3_at AATGCAGTGTTTTTCTTGTGTGTCC SEQ- ID NO:921 WBCOOlBl1_V1.3_at GAGACCACTGGTCATTCATTACCTG SEQ ID NO:922 WBCOO1B11_V1.3_at GTAGAATCCCACTTTTGCTTTCTTT SEQ ID NO:923 WBCOO1B11_V1.3_at GGAAGACCAATCTATCACCTTGAGT SEQ ID NO:924 WBCOO1BlVl.3_at TGTGACTGTCATCCTAGCCTTTTAA SEQ ID NO:925 WBCOOlB11_V1.3_at TCTGGTGTATTTTGGTTCTCTTGGC SEQ ID NO:926 WBCOMl11_V1.3 at TCAAGTTTCATGTGGCCTGGGTGTT SEQ ID NO: 927 WBCOO1C11_V1.3_at ATCTATTTTCTTCAAACTTCTGCAA SEQ ID NO:928' WBCOO1ClV1*.3_at AGCTGACTTTTTTATGTGCTCTAAA SEQ ID NO: 929 WBCOO1Cl1_V1.3_at AGCTCTTTAATCTCTTTATAAGTTA SEQ ID NO: 930 wBcoo1ci.1_V1.3_at A AACAGTTGGTTAGCAAGCTGACT SEQ ID NO: 931 WBO1C1lV1.3_at IAACTGGATCTCCAATTGATATTTTC SEQ ID NO:932 -361- POBE A~1IC~ eune ____ ____ ____ ____ __ * -. dent~i eV WBCOOIC11_VI. 3_at GCCAGTCCCTGACATATCATGGAAA SEQ ID NO: 933 WBCOO1C11_V1.3_at GACTTGTTTCAAGCTCTTTAATCTC SEQ ID NO:934 WBCOO1C11_V1.3_at GAGTGCTTTCATTTTGATAACTGGA SEQ ID NO: 935 WBCOOIC11_V1.3_at GTATAACT.CATTTGCAGTCTGGAAA SEQ ID NO: 936 WBCOO1Cl1_V1.3_at GGCACAAATTTCTTTTTAAGACTTG SEQ ID NO: 937 WBCOO1C11-V1.3 at TTTTTTAGTGCCAGTCCCTGACATA SEQ ID NO: 938 WBCOO1C11 V1.3_s-at ATGCCTGCTTAGTGCTTTCTGATTA SEQ ID NO: 939 WBCOO11_1.3_s-at ACTCGCATTCTGTTTCTTGCTTTAA SEQ ID NO: 940 WBCOO1C11_V1.3_s-at ACACACACTCATGGGATTCCAGTTA SEQ ID NO: 941 WBCOO1C11_V1.3_s-at TCTTTGCAAGTGCTTTTGGAACTAA SEQ ID NO: 942 WBCOO1C11_V1.3_s-at CCCCACAATGATTTTCTTTGCAAGT SEQ ID NO:943 WBCOO1C11_V1.3 s-at GCTTTCTGATTACTCGCATTCTGTT SEQ ID NO:944 WBCOO11_1.3 s-at GCAGTTCTGTAGTGTCATTTCTTAT SEQ ID NO:945 WBCOO1Cl1_V1.3_s at GATTCCAGTTATTACGAGTTGCTTT SEQ ID NO: 946 WBCOO1C11_V1.3 s at GTTGGATCAGTATTGCAGTTCTGTA SEQ ID NO: 947' WBCOO1C11_V1.3 s-at GTTTAAAGCCTAACACCATTCTAAT SEQ ID NO:948 WBCOO1C11_V1.3_s~at. TCTTGGATTAACTGATGCCTGCTTA SEQ ID NO: 949 No Homology WBCOO1C12_V1.3 at ATTACTCACTTTTCACTTCTATCTA *SEQ ID NO:950 WBCOO1C12_V 1.3_at AGTCAACTCCAMATTCTCATTCTTC SEQ ID NO:951 WBCOO1C12_V1.3_at AGAATGACTGTTGGAGGCCGGCCCA SEQ ID NO:952 WBCOO1C12 V1.3_at ACATGCTGTGCTTTGGTGGCCTAGG SEQ ID NO: 953 WBCOO1C12_V1.3_at AATGACCCAACCCTGTATTTATGCA SEQ ID NO: 954 .WBCOO1C12_-V1.3_at AATAATCAACAGTCTTCCCTTTCCT SEQ ID NO: 955 WBCOO1C12_V1.3_at GGGCTATAACCCCAACATATCGTGA SEQ ID NO: 956 WBCOO1C12_Vl.3_at GGGTGTAGACCGACACAGCACGCAT SEQ ID NO: 957 WBCOO1C12_V1.3_at GGAAGCTCTTATTGGGCATATCTGC SEQ ID NO: 958 WBCOO1C12_V1.3_at TGTGGGCTCAGCATGAAGTCAACTC SEQ ID NO:959 WBCOO1C12_V1.3_at TGCTGTGGCGGCATTCCATGTAGAA SEQ ID NO: 960 RAB1O, member RAS oncogene family (RABlO), WBCOO1FO8_-V1.3 at AAGTCTCTTGGGATCCTGTGTAGAA SEQ ID NO: 961 WBCOOIF08_-V1.3_at AATTTTACTGTCTTGTTGCTTTCCT SEQ ID NO: 962 WBC0O1FO8 V1.3 at GTTAAGTCCATTCTCTGGTACTAGC SEQ ID NO:963 WBCOO1FO8_V1.3_at GCAGCATTGCCAAATAATCCCTAAT SEQ ID NO:964 WBC0O1FO8_V1.3_at GTTGCTTTCCTTCATCTGGAATGTG SEQ ID NO:965 WBCOO1FO8_V1.3_at GGTACTAGCTACAATTCGGTTTCAT SEQ ID NO:966 WBCOO1FO8 Vl.3_at .GGCTACCTTTTGTTAAATCTGCACT SEQ ID NO: 967 WB.COO1FO8_V1.3_at TTGCCCCTTTTTCTGTAAGTCTCTT SEQ ID N6:968 WBCOO1FO8_V1.3_at TATGCCTCACTGGTGGTTGTTCTTA SEQ ID NO: 969,. WBCOO1FO8_VI.3_at TtTGCTTAATATTAGGGCCTTGCCC SEQ ID NO:970 WBCOO1FO8_V1.3_at TTTCCCTCACTTGACTTTATCATTG SEQ ID NO:971 Retinoblastoma-like 2 (p130) _________________ ______ __ WBCOOlF11_V1.3__at ATTAAGAGGGATCAGCTGGCTAAGT SEQ ID NO:972 WBCOO1F11_V1.3_at IATATCTTTGAGTGTGTTCCTGGCAG SEQ ID NO:973 -362- Ptobe, Set' ameo Wi PROBE Bqecj WBCGO1F1_V1.3_at ATCTTCTTTGATGCTTTTGTACTTT SEQ ID NO:974 wBcO01F1lV1.3_at TTGTTAAAGCCCCAGTAGCCACCTT SEQ ID NO:975 WbCOO1F1lV1.3_at AAATTATGACCTCTTCCTTTAGGAG SEQ ID NO:976 WBC001F11_Vl.3_at AAACCTCTCAGATACTGCTACTGTA SEQ ID NO:977 WBCO01FMl_1.3_at, GCTATTGTTCCAGCAGTTTTAACGT SEQ ID NO:978 WBCOO1F11_V1.3_at GAAATTCTCCAGTTTTTGATTATTA SEQ ID NO:979 WBCO0lF11_v1.3_at GTAGCCACCTTTTGGGCATATTTGA SEQ ID NO:980 WBCOO1F11_V1.3_at TACTAGGTAACTTCACATTGCTCTG SEQ ID NO:981 WBCOO1F11_V.3 at TATACACCTTTATTAATCGCTATTG SEQ ID NO:982 Activated RNA polymerase II transcription cofactor 4 variant protein (incomplete) WBC001HO9_V1.3_at ATTTCCCGTACTCTTGGCATTTTAT SEQ ID NO:983 WBCOO1HO9_V1.3_at GAATACTCCTACCTCATTAGCTAGT SEQ ID NO:984 WBC001HO9-Vl.3-at AAGAGTGTGTACATCCTGGCTTGGC SEQ ID NO:985 WBC001H09_Vl.3_at AATTGTGGAATACCTGTCTGCTTTG SEQ ID NO: 986 WBC001H09 V1.3 at GGAGTAAACATTCACGTAGTCACAA ISEQ ID NO:98 WBCO 00HO9_V1.3_at GAAATTCTTTGCAACTOTCTTTTTA SEQ ID 'NO:*988 WBCOO1HO9_V1.3_at 'GATTAACCTATTCTACATAACGTGT S EQ ID NO:989 WBCO0lHO9 Vl.3 at GATTATTCTCTTTTGTTTTGCTTCA SEQ ID NO:990 WBCO-01H09_V1.3 at GTCTGdTTTGTTTGGTACATCTTCC SEQ ID NO:991 WBCO01HO9 V1.3 at TGTTTTGCTTCATCAATGCCTAAGA SEQ *ID NO.992 WBCOO1H09_Vl.3_at TACAAGCAGCATTTGACCCATTTCC SEQ ID NQ:993 No homology WBCOQ3D1l_V1.3_at ATCTTCATTTQCTCTTAGCTGTCAG SEQ ID NO:994 WBCOO3Dl1_V1.3 at AGACAGAGTGTGCATTCCTTCTTGC SEQ ID NO:995 WBC0OD11_V1.3 at CATCGGACCAACTTGTAGCTGACTA SEQ IDNO0:996 WBCOO3D11 Vl.3 at AATGTGCCCAGGCTGAACTGCTGGA SEQ ID N0:991 WBCOO3D11_Vl.3 at CGATAAGTCTCGCTTGTTCTTGCAC SEQ ID NO: 998 WBCOO3D11_V1.3 at GAGGTTGTCCTTAATCAGCCATCGG SEQ ID NO: 999 WBCOO311_Vl.3_at GAGGGTGATTCGCATCTTCATTTCC SEQ ID NO:1000 WBCOO3D11_Vl.3_at GTCACATCCATGAGCCCAGTCAAGA SEQ ID NO:1001 WBCOO3D11 Vl.3 at GTCATTCCATTATACCAGCTGAGGT SEQ ID NO: 1002 WBCOO3D11_Vl.3_at TATGGCTTGGCCTTGAGACTTGCTT SEQ ID NO:1003 WBCOO3D11_Vl.3_at TTCTTGCCCGTTACACGATAAGTCT SEQ ID NO: 1004 ZER, domain containing WBCOO3FO2_V1.3_at ATGTGCCAGACATCACCTCAGATGA SEQ ID NO: 1005 WBCOO3FO2_V1.3_at AGCAAGCCTTGGGACATCAGCCTGG SEQ ID NO:1006 WBCOO3FO2_V1.3_at CCTGGCCTGTGCTTTACTACAATGA SEQ ID NO:1007 WBCGO3FO2_V1.3. at GCCCTAGAGGGTGTCCTTGTGTGAA SEQ ID NO: 1008 WBCOO3FO2_V1.3_at GAAGCACACTTGTTATGCACCTGCT SEQ ID NO: 1009 WBCOO3FO2_V1.3_at GAAAGACTGTTTGGCCAGCAAGCCT SEQ ID NO: 1010 WBC003FO2_V1.3_at GAGAGCATCCGCAGTGACCTGGAGA SEQ ID NO: 10.11 WBCOO-3FO2_V1.3_at GATTCTTATCTCATGGGCACTGTAG SEQ ID NO: 1012 -363 at.4(PRbE E SeENuEence - *~4 1 *~.* Identifier WBCO03FO2 V1.3 at GGATTGAATGCTCCTGTTCTGAGAA SEQ ID NO:1013 WBC003F02 V1.3 at GGCACTGTAGCCAGACTTAGCACAT SEQ ID NO1:1014 WBCOO3F02 V1.3 at TGGAGAGCTCCGATACGCAGTCAGA SEQ ID 1.1:1015 CGI-54 protein WBCOO3H1 V1..3 at ATATCAACATGACCCACTACATTCG SEQ ID NO1:1016 WBCOO3HO1_Vl.3 at ATGACTTGCAGAGCTTCGGCCTCGA SEQ ID NO:1017 WBC003H01_V1.3 at ATGACCCACTACATTCGGCACCTGT SEQ ID NO:1018 WBCO03HO1_V1. 3 at AGAGCTTCQGCCTCGACAATATCAA SEQ ID NO:1019 WBCOO3H01_Vl.3 at GGGQATTGTGAACCCCCTGGACCGC SEQ ID NO:1020 WBC0O3IIO1_V1.3_at ACGTCCATGACTTGCAGAGCTTCGQ SEQ ID NO1:1021 WBCOO3HO1_V1.3 at CTTCGGCCTCGACAATATCAACATG SEQ ID NO:1022 WBCOO3HO1_V1.3_at CTACATTCGGCACCTGTCATTCGGG SEQ ID NO:1023 WBCOO3HO1_V1.3 at GCAQGTCCATGACTTGCAGAGCTTO SEQ ID NO: 1024 WBCOO3HO1 V1.3 at GGAGGACtACCCGGGCATTGTGAAC SEQ ID 1.1:1025 WBCOO3HO1_V1.3_at GGCCTCGACAATATCAACATGACCC SEQ ID N0:1026 Heterogeneous nuclear ribonucle oprotein F WBCO04BO5 V1.3_at ACtGTGATTTCTTTTTGGGTGTATT SEQ ID 1.1:1027 WBC0,04B05 V1.3 at ACATTTCTCATGTTTGTTCATTCTA SEQ ID NO:1028 WBCOO4B05 V1.3_at AAACTTTCTTTGTACTGTGATTTCT SEQ ID NO:1029 WBCOO4BO5 V1.3 at GAAAACTCAAGGTGCTAGATCCCTA SEQ ID NO:1030 WBCOO4BO5_V1.3_at GAGACGTGCTTTTTTGGAAAACTCA SEQ ID 1.1:1031 WBCOO4BO5_V1.3_at GAGACACATTACTAATACTGTAGGA SEQ ID NO: 1032 WBCOO4BO5 V1.3 at GGGTGTATTTTOCTAAGTGAAACTT SEQ ID N.1:1033 -WBCO04BO5_V1.3_at GTTCATTCTAGTTTATTTTCATTTA SEQ ID 1.1:1034 WBCOO4BO5_V1.3_at GTGAGGCCTTGACTTAAAACTTTCT SEQ ID NO:1035 WBCOO4BO5_-V1.3 at GGTGCTAGATCCCTAA-TTCGAAGAG SEQ ID NO:1036 WBCOO4BO5_V1.3_at TTACACCACATCACCGTGAACACAT. SEQ ID 110:1037 WBC0O4BO5 V1.3 s at ATTACCTCTTCAGTGTTTTCTCATG SEQ ID N0:1038 WBCOO4BO5_V1.3 s at AAAGCAGTTAACTCTAGAGGGAGCT SEQ ID 1.1:1039 WBCOO4BO5_vl.3-s at AAQATTTTGGTAGTGTACTTCAGAG SEQ ID 140:1040 WBCOO4BO5_V1.3_s at GCAAACTTTCTTCTAGCATGTGATA SEQ ID 140:1041 WBCOO4BO5_V1.3_s-at GGAGCCATTTTGCACCATGAGTTTG 'SEQ ID NO: 1042 WBCOO4BO5_V1.3_s-at GGAGCATTTGAGTTGTTTCAATCAA SEQ ID 1.1:1043 WBCOO4BO5 Vl.3 a at TGTGGATCTTTTACACGACATCACC SEQ ID 1.1:1044 WBCOO4BOSV1.3_a-at TAGAGGGAGCTGTGGGACCCATTTT SEQ ID 1.1:1045 WBC004B05_Vl.3_s~at -TTCAGCTTTTCT.CAATTAACATTTT SEQ ID 1.1:1046 WBCOO4BO5_V1.3_s at TTTTCTCATGCAAACTTTCTTCTAG SEQ ID 1.1:1047 WBCOO4BO5_V1.3_a-at TTCAATCAAATTTTCACAGGCAGCC SEQ ID 140:1048 Dendritic cell protein variant, clone: CAE03 638 ________________ WBCOO4CO3_Vl.3_at ATATCTTGGCTTTTCCTTGTGTGAG SEQ ID NO:1049 WBCOO4CO3 1.3 at ATGTTTCCGCTCATGCTTCAGAGTA SEQ ID 40: 1050 WBC004003_-V1.3_-at AGGCACTGCATTGGGTCATACTTAA SEQ ID 140:1051 WBC004C03_Vl.3_at AAATCTGTTTTGTCTTCTACTCCCT SEQ ID NO: 1052 WBCOO4CO3 V1.3 at ICTACCTTTTACTTCATGTTTCCGCTSEIDO:15 -364- PrOe St;Nais~ IPROBE S1.4 TE -. sequence - '. ffi. dentifier WBCOO4CO3_V1.3_at GAGAGACCTGTCAACATTTTGTTAT SEQ ID NO:1054 WBCOO4CO3_V1.3_at GTTATTGTTTGCTGCTAGTCGCTTT SE'Q I D N6:1055 WBCOO4003_V1.3_at GTAATCCACTATCCAGAQAGACCTG SEQ I D NO:1056 WBCOO4CO3_V1.3_at GTGGCATGTTTCCAAGGCACTGCAT SEQ I D NO:1057 WBCOO4CO3_-V1.3_at TGTTTTGTATCTTCTGTCAGAGCCA SEQ I D NO:1058 WBC004CO3_V1.3 at TTCCCTTCCCAAACATGTCTATGTT SEQ I D NO:1059 No Homology WBCOO4DO7_1.3_at ATCCATCCCACAGTCAACTGGTTGA SEQ I D NO: 1060 WBCOO4DO7_V1.3 at AGTTTGCTGGCCAATTGCACCTGCT SEQ I D NO:1061 WB .COO4DO7_1.3 at ACCTGCTGTGTTGTTTTCCATCCAT SEQ I D N'O:1062 WBCOO4DO7_V1.3 at AAACGGTCTGTGATTTTGGAACTGG SEQ I D NO:1063 WBC004 D07_V1.3_at CATACCTTCTCATGTGCATTTCAGT SEQ ID*NO: 1064 WBCOO4D7 V1.3 at GAAAGACTTCTTAGCGTTCCAGTTT SEQ I D NO:1065 WBC00D7_V1.3_at GACTGTGGCACACTGATGCACTGAA SEQ I D NO:1066 WBCOO4DO7 V1.3_at GAGTCATGGATTTCTTTGCTTACAA SEQ I D NO:1067 WBCOO4D7_V1.3_at GTAACACCATTTTTCTTTGAGACTA SEQ I P NO:106B WBCOO4DO7_V1.3_at GTGGCTGCAGGAATTCTTTTCTAAA SEQ I D NO:1069 WBCOO4DO7_V1.3_at TTATTTCTCCCCATGACTTCAAACA SEQ I D NO:1070 TRAP-interacting protein with a forkhead-associated domain_________________ __ WBCOO4EO4_V1.3 at ACGAAGTGGTGTGCCGGTACTGATC SEQ I D NO:1071 WBCOO4_1.3_at CAACGGTCATTTGTTTTCAAGGTCA SEQ I D NO:1072 WBCOO4EO4_Vl.3_at ACTAGTGTTGTAGCCTGTTGGTACT SEQ I D NO:1073 WBCOO4EO4 Vl.3_at AAGrAACTCTCTCTTGGTTTGGTCA SEQ I D NO:1074 WBCOM4_1.3_at GTTAGTCATCGATTTGGTCTCCTGT SEQ I D NO:1075 WBC004E04_Vl.3 at GTACTTATAGTACCAGTGTCCTGGA SEQ I D NO:1076 WBCOO4EQ4_Vl.3_at GGTCATATTATTTCACAACGGTCAT SEQ I D NO:1077 WBCOO4EO4 V1.3 at TQTTATTGTTATCTGCTQTQCTGGC SEQ I D NO:1078 WBCO4EO4V.3_at TCTCCTGTTGCATTCCTGGATGTAT SEQ I D NO:1079 WBCOO4EO4_V1.3 at TCCCCTTCGTTACTGTGGTATGTTA SEQ I D NO:1080 WBCOO4EO4_V1.3 at TAGACGCTCCGCTTACGAAGTGGTG SEQ I D NQ:1081 WBCOO5BO9 V1.3 at GCGCTGTAAGCCTCTGAAGGAATTT SEQ I D NO:1082 WBCOO5BO9_V1.3 at GAATTTATGCTTTCTCAAGATGCTG SEQ I D NO:1083 WBCOO5BO9_V1.3_at GACCr7ATTGGACTGGGATGAACATA SEQ I D NO:1084 WBCOO5BO9_V1.3_at GATGCTGAACATGAGCTGCTCTTTG SEQ I D NO:1085 WBCOO5BO9_Vl.3_at GTATTGCCGTGTTTATTTTGCTTAA SEQ I D NO:1086 WBCOO5BO9_V1.3 at GTAAATATTTCCATCATGACCGA TT SEQ I D NO:1087 WBC005BO9_-V1.3 at GGGTTTACAGTATTTCCAACACATG SEQ I D NO: 1088 WBCOO5BO9 V1.3_at GGAGATATGTTTCAAGGCGCTGTIA SEQ I D NO:1089 WBCOO5BO9_V1.3_at TGAGCTGCTCTTTGACCTCATTGAG SEQ I D NO:1090 WBCOO5BO9_V1.3_at TCCCAACCATGTGATGTCTGOAGTA SEQ I D NO:1091 WBCOO5BO9_V1.3_at TAAAGCATCCTTTCTTTTACCCTCT SEQ I D NO:1092 Homo sapiens hypothetical protein I_______________ -365- -1PRO BE EQUN9O ~equence % FL322662, mRNA WBCOO5DO2_V1.3-at ATCTTCCGGCGCGACCAAGGGAAAG SEQ ID NO: 1093 WBCOO5EPO2_V1.3_at ATCTGCTGCCGTGAGGACCTGAACT SEQ ID NO: 1094 WBCOO5DO2_V1.3 at ATGCCAGAGGCCTACAACTTTGATT SEQ ID NO: 1095 WBC00D2_V1.3_at AGTCCTGGAGGCTGCTACGATACGA SEQ ID NO: 1096 WBCOO5DO2_V1.3_at ACAGCCTATGCCATTAGTGGTCCCA SEQ ID NO: 1097 WB0005D02_V1.3_at AGCTGGGTTTGGACTTCTCTTATGA SEQ ID NO:1098 WBC005D02_Vl.3_at ACCGGTTCAACAAAACTCTCCATGA SEQ ID NO:1099 WBCOO5DO2_V1.3 at AAATCTACAACTGGAGTGGCTACCC SEQ ID NO:1100 WBCOO5DO2_V1.3_at GTGGCTACCCAATGCTGGTTCAGAA SEQ ID NO:1101 WBCOO5DO2_V1.3 at GTGGTCTCCCTGTTTTTCACTGGMA SEQ ID NO:1102 WBCOO5DO2_V1.3_at TTCTCTTATGATCTGGCTCCACGAG SEQ ID NO:1103 Polymeric imnunoglobuli.n receptor 3 precursor (PIGR3) _ _ _ _ _ _ _ _ _ _ _ _ _ _ _ WBC0O5F1OV1.3_at TTTCGACTGGCGCAACGTTTGGTAA SEQ ID NO:1104 WBCOO5F1OV1.3_at ATAACTTTTGTACCGTGCCCTCTAT SEQ ID NO:1105 WBCOO5F1OV1.3 at AGTGGTTAAGGCTTCCTATCCAGAA SEQ ID NO:1106 WBC0O5F1OV1.3 at AGCCCAGCTTCCTGAGTACCAATAA SEQ ID NO:1107 WBCOO5F1O V1.3 at CAGTGACTGACCCATATGTAGCAAA SQI O10 WBCOO5F1OV1.3_at GCCTGCAQCGTGAGAAGACTTCCCA SEQ ID NO:1109 WBCOO5F1OV1.3_at GCTGCTCACTCACTGTGGGATGTTA SEQ ID NO:1110 WBCOO5F1OV1.3_at GATAATACCCACTTTCTAGGATTGT SEQ ID NO:1111 WBCOO5F1OV1.3 at GATGTTATGAAAGCGACCCTTCCAA SEQ ID NO:1112 WBCMOF1O V1.3_at TAACGTTTGACCCTGAGGCCCAGAG SEQ ID NO:1113 WBCOO5F1OV1.3_at TTCCTTCTGGATCGTTTCTCCMAGA SEQ ID NO:1114 Homo sapiens methionine adenosyltransferase II, beta (MAT2B) _______________ WBCOO6EO3_-VIA.3_at ATAMAACTGTCCTTTTCACTCCATG SEQ ID NO:1115 WBCOO6EO3 V1.3 at AGGTTTTTATGCTCGAGATCTTTCG SEQ ID NO:1116 WBCOO6E03_V1.3_at ACAGATCTGCTGTAGACTTGTTTTT SEQ ID NO:1117 WBC006E03_Vl.3_at GTATATTGGAACTCCTGCAGCTTrCG SEQ ID NO:1118 WBCOO6EO3 V1.3 at TGGCTTAACTCGCTGTTTGCGTATA SEQ ID NO:1119 WBCOO6EO3_Vl.3_at GGCCTTGTAAGTCTTTTGACCATTC SEQ ID NO:1120 WBC006EO3_Vl.3_at TGCTCTTGCGCTAGTGAAATGGTCT SEQ ID NO:1121 WBCOO6EO3_Vl.3 at TTTGCAAOTGTTGACCCTTTTATGT SEQ ID NO:1122 WBCOO6EO3_V1.3_at TGCATCGTTCATTCCTATAAGCTCT SEQ ID NO:1123 WBCOO6EO3 Vl.3_at TATTTGCTTTGCCTGAGCTCAGATC SEQ ID NO:1124 WBCOO6EO3_V1.3 at TATCATTTTGTTTGTTCTGGCTTAA SEQ ID NO:1125 Ubiquitin-coni ugating enzyme E2E (RAD6 homolog) (UBE2B) ________________ WBC006H06-Vl.3-at ATTCACAATTTGCACCTCTATCATG SEQ ID NO:1126 WBCOO6HO6_V1.3_at AGGCTACTTGTTACTGTTTCTTCAT ---- SEQ ID NO:1127 WBCOO6I-6V1. -3_at ACAAGCTATCCTATGCCTTCAAATA ISEQ ID NO:1128 -366- Probe Set Narneq : PROiBE SEUN Seue "Identifier.' WBCOO06HO6V1.3 at AATGTTTTAATACTAGGGCCTGCTG SEQ ID NO: 1129 WBCOO6HO6_V1.3_at AATCCATGCCCCACTATTAACAATG SEQ ID NO:1130 WBCOO6HO06 Vl.3 at MTTGGCACQTCTACCTTGAGCAGA SEQ ID NO: 1131 WBC0O6HO6_V1.3 at GCTGAGTTGCTTTCTCTTGTGGAGA SEQ ID NO: 1132 WBCOO6HO6_V1.3 at GCAATTGCCTATCTGTTTATTCTGG SEQ ID NO: 1133 WBCOOa66V1.3_at GTTAAACTGTACCTTTTGCGATTCA SEQ ID NO:1134 WBC0O6HO6_V1.3_at GTTTCTTCATGCACTACTTACTGTT SEQ ID NO: 1135 WBCOO6HO6 V1.3_at GTCTGTCCMACTCTGTATTTAGGCT SEQ ID NO:1136 No homology WBCOO7AO9_V 1.3_at ATCAATCCAGCAATCTGAGCGCTTC SEQ ID NO:1137 WBCOO7AO9_V1.3_at AGGGCTTATGCTATTTCCTGTTTCT SEQ ID NO:1138 WBCOO7AO9_V1.3_a t AGCATCATGTCTCACTTGGGTTACT -SEQ ID NO:1139 WBCOO7AO9_V1.3 at GAATTCTACTTCTGGCTAGGGCTTA SEQ ID NO:1140 WBCOO7AO9_V1.3 at GAGGTCTCCTTGATCCTTTAGTATA SEQ ID NO:1141 WBCOO7AO9_V1.3 at GGMCGTTCTACTAGGCGCTACATG SEQ ID NO: 1142 WBCOO7AO9_V1.3_at TGAGCGCTTCTCAGGACTGTACTAC SEQ ID NO:1143 WBCOO7AO9_V1.3_at TAAGATGTGTGTTGTCTCTTTCCCT SEQ ID*NO: 1144 WBCOO7AO9 V1.3 at TATGATCTTTCCTCAAGTGTCACCT SEQ ID NO:1145 WBC007A09_Vl.3_at TTCCTTGCTTCCTTTAACACACGAA SEQ ID NO:1146 WBCOO7AO9_Vl.3 at TTGGGTTACTGCAGTAGCTCCCTGA SEQ ID NO: 1147 Transmembrane protein 23 WBCOO7GO3 V1.3_at ATTAGTTATCCATACTCTCATGACA SEQ ID NO:1148 WBCOO7GO3 V1.3_at ATATCCATTCTGTATTTTACGTGCA SEQ ID NO:1149 WBCOO7GO3_V1.3_at CATACTCTCATGACAATTTTGTTGG SEQ ID NO:1150 WBCOO7GO3_V1.3_at CTGATATCTTAACAGCTTACCTAGA SEQ ID NO:1151 WBC0O7GO3_1.3 at GCAGAATTATCTTCCGTAGGGTTTT SEQ ID NO:1152 WBCOO7GO3_Vl.3_at GTGCAGAAACTGCATGTAATTCTAA SEQ ID NO:1153 WBC007GO3-Vl.3-at TTACGTGCAGCAGAATTATCTTCCG SEQ ID NQ:1154 WB007G3_V1..3_at GTGTTCACATTCGTCACAAAGTTGT SEQ ID NO:1155 WBC007G03_V.3_at GGCTCTTATTTCTAATGTGTTCACA SEQ ID NO:1156 WBCO7GO3V.3_at TTCTAAGTTTTACTCCTAACATAAG SEQ ID NO:1157 WBCOO7GO3_V1.3_at TTCTATTCTATACTTGCCAATGTGG SEQ ID NO:1158 No Homology _______ WBC07G2_V1.3 at ATGTGTGTACTGTATCTGCCTTTCC SEQ ID NO:1159 WBCOO7G12_V1.3 at AGTTGTGCAGTTTTTCTTTTCAGAA SEQ ID NO:1160 WBGOO7G12_Vl.3_at ACTGCCTGCTTTTTTGACCTTTGTT SEQ ID NO: 1161 WBCOO7G12 V1.3_at ACTGATTACTGTGTCTTGCTCTTCG SEQ ID NO:1162 WBC0O7G12-V1.3 at AACAGTGATCCTAGGGCTGACCGCA SEQ ID NO: 1163 WBC0O7G12 V1.3_at GCAGCCTCTTTTGCATAGTCATGTA SEQ ID NO:1164 WBCOOIG12_V1.3_at GGATTCAGTCTTGTCTTTTGTCTAG SEQ ID NO: 1165 WBCOO7G12_V1.3_at TGTTCATACAATGTGGCAGCCTCTT SEQ IV NO:1166 WBCOO7G12_V1.3 at TGCCTTTCCACCACATTTTTATGAC SEQ ID NO: 1167 WBCOO7G12_V1.3_at TTATGACACTGTATTCCACTGCCTG SEQ ID NO: 1168 WBCOO7G12 V1.3_at TTGTTCCCTCGGATTTGTCCTATAA SEQ ID NO:1169 WBC008DO5_V1.3_at ATGCCCATGGAACATTCTCTAGGAT SEQ ID NO: 1170 -367- Prb~Se i 1 ~~ ~.PROBE SQNI. ?sequen64' V' ~ ~~*~:* 7 ?;~ ~ ' ~ Identifier. WB3COQ8DO5_V1.3_at AGGATTGATCACATATTAGGCCACA SEQ ID NO:1171 WBCOO8DO5_V1.3 at AGAACATTCCATCCAAAAACCACAG SEQ ID NO: 1172 WBCOO8DO5 V1.3_at ACACATTCTTTTTACATGCCCATGG SEQ ID NO: 1173 WB0008D05_V1.3_at AATACCATGCAGCTTTTCTGACCAC SEQ ID NO:1174 WBC008DO5_-V1.3 at AATATCTATGCACCCAACACAGGAG SEQ ID NO: 1175 WBCOO8DO5_V1.3_at GCAGCTTTTCTGACCACAAAGGTAT SEQ ID NO:1176 WBCOO8DO5_V1.3_at TAAGAGACAAAGACGGGCACTACAT SEQ ID NO: 1177 WBCOO8DO5_V1.3_at GAAACACTCGCCTGAAA~GGACACAT SEQ ID NO:1178 WBCOO8DO5_V1.3_at TTTAACACTCCACTTACACCAATGG SEQ ID NO: 1179 WBCOOBDO5_V1.3_at TTAGGCCACAAAACAAGTCTCAATA SEQ ID NO:1180 No Homology WBCOO8FO6_V1.3_at ATATTTCTGATTGGTGCCTTTCCAC SEQ ID NO: 1181 WBCOO8FO6_V1.3_at AGTTGGTTATAGTCTTCTGTTCTGA SEQ ID NO:1182 WBCOO8FO6_V1.3 at CAACCAGCTCGGACATTTGTOTTTT SEQ ID NO:1183 WBC08F6V1.3_at CATAAGCCGTTTTTCTGTTTAATGG SEQ ID NO:1184 WBCOO8FO6_V1.3_at GCCTTTCCACTTTTTAGCAGCAATG SEQ ID N.1:1185 WBCOO8FO6_V1.3 at GATGTTTTCGTTCCCWATGTGACT SEQ ID NO:13.86 WBCOO8FO6_Vl.3_at GTTATCTGCTTTCCTTCATTTTTGA SEQ ID NO:1187 WBCOO8FO6_V1.3_at TGTCATAAACCCCATCATAAGCCGT SEQ ID NO: 1188 WBCOO8FO6_Vl.3_at TGAAATTCTTTCATGTCGTTTCCCT SEQ ID NO:1189 WBC008FO6_Vl.3_at TTTCACTCATGCCAAAACAACCAGC SEQ ID NO:1190 WBCOO8FO6 V1.3 at TTTGAGCCTGTTATTCGACACCATC SEQ ID NO:1191 v-ral simian leukemia viral oncogene homolog B (ras related; GTP binding protein WBCOO8F12 V1.3_at AGGGCCTCTTCTCTGTTTGTTTCAG SEQ ID NO:1192 WBCO8F12_V1.3_at AGTGTGACATGGGTTCTTCTGAAGA SEQ ID NO:1193 WBCOO8F12 V1.3_at AGACATCTGCTACCTCTCGTAGGAT SEQ ID NO:1194 WBCOO8F12_-V1.3_at AAAACCCAGTATTCAGCACATGTCC SEQ ID NO:1195 WBCOO8F12_V1.3_at CTCCGAGAATTGGTTGCTGTTTAGA SEQ ID NO:1196 WBCOO8F2V.3_at GAAGGATGCGATAAGCCGTTGCCCC SEQ ID NO:1197 WBCOO8F12 -V1.3_at TGCACCTGGAGCTTGAGAGGGCCTC SEQ ID NO1:1198 WBCOO8Fl2_V1.3_at GATTGCCCCGTAATTCTAAATTTAG SEQ ID NO:1199 WBCOO8F12_V1.3 at GTTGTGTTCCAAAGTCCTGAAGCCA SEQ ID 1.1:1200 WBCOO8F12 -V1.3_-at TGGAAAGCATCTTGTATCTCCTCCC SEQ ID NO:1201 WBCOOMF2_V1.3_at TGAAGCCAGAGCCTGCGCCAGACAT SEQ ID NO:1202 Human mRNA for complement receptor type 1 (CR1, C3b/C4b receptor, CD35) _______________ _______ WBCOO9B1O V1.3 at ACTGTGTTCAGCCTCAAAGTCTGCA SEQ ID NO:1203 WBCOOB1O1.3_at CTCATAGTCGGCATATTCTTCGGTA SEQ ID NO:1204 WBCOOSB1O_1.3 at CTTCGTTCTCTGGATTTGTCTGTAT SEQ ID NO:1205 WBCOO9B1OV1.3_at CTGGTTTCCTCCAATGAACTGCTTA SEQ ID 140:1206 WBCOO9B1O_-V1.3_-at GCTTACAGCCCCAGCAAGAGAGGAA SEQ ID NO:1207 WBCOO9B1OV1.3_at GCAATTCCTCTGTTATTTCCTAATA SEQ ID 140:1208 WBCOO9B10_V1.3_at GTATGATCTTCTTTATTGTACCCAT SEQ ID 140:1209 -368- -I-, Probe: sdt,* PROBE EQUENCE;' : **~"*. -. .. '.-: ~Identifier WBCOO9B1OV1.3_at GTGATTATCCATTTACATCCCCAAC SEQ ID NO: 1210 WBCOO9B1O_V1.3 at TACATCCCCAACAAGGCAACTGTGT SEQ ID NO:121. WBCOO9B1O V1.3_at TAGTTTCCACGTCCCAAATTGCAAT SEQ ID NO: 1212 WBCOO9B1O_V1.3_at TTGTACCCATCATTATTTCCTGTTG SEQ ID NO: 1213 Down-regulator of transcription 1, TBP binding (negative cofactor 2) ________________ WBCOQ9E12_V1.3_at ATTAAATACATTTCTCCCATGCCAC SEQ ID NO:1214 WBCQO9E12_V1.3_at AGGATAGATTTCAGCTCCCAGGATC SEQ ID NO:1215 WBCQO9E12_V1.3_at AGTGTTGGACTTCTTAATGATCATA SEQ ID NO:1216 WBCOO9E12_V1.3 at AGCTCCCAGQATCCCAATTTTAATT SEQ ID NO:1217 WBC0O9E12_V1.3_at AATTTCTGTATTCACCAAGCCCAAG SEQ ID NO:1218 WBCOO9E12_V1,.3_at GACATTCTTGTGATTTCATATGCTG SEQ ID NO:1219 WBCOO9E12_V1.3 at GTTCGAAGCCTGGTGACTTTTCATT SEQ ID NO:1220 WBCOO9E12_V1.3_at GTAATCTAAATTCCTGTGTOAGTTG SEQ ID NO:1221 WBCOO9E12_V1.3 at GTACTGTAACATCCTTAtACTTTAT SEQ ID NO:1222 WBCOO9E12_V1.3_at GTGTTGGCTTTTCTAATTTGTACTG SEQ ID NO: 1223 WBC0O9E12_V1.3_at GTGTCAGTTGCCAAATCACTTAAAT SEQ ID NO:1224 3-hydroxy-3 methyiglutaryl Coenzyme A synthase, 1 (soluble) ________ WBCO1OFO4_V1.3 at ATGACATGAGCCTTATAGACTGTAA SEQ ID NO:1225 WBCO1OFO4 V1.3 at AGTGCATTGCCAGCAGTGGGCAGGC SEQ ID NO:1226 WBCO1OFO4_V1.3_at AATTACTTCATTTTAACATCCACTG SEQ ID NO:1227 WBCO1OFO4_V1.3_at CACCTTATTAACTGTGAGGTCATAA SEQ ID NO:1228 WBCO1OF04 V1.3 at GCAGGCCTGGCATTATTGGCACAGA SEQ ID NO:1229 WBCO1OFO4_V1.3_at GAGCATTAACTGTGCACCTTATTAA SEQ ID NO:1230 WBC01OFO4_V1.3 at GATCTCTTTGGTGCTGAACTATGAC SEQ ID NO:1231 WBC1OF4V.3_at GGGTGTCAGGAAATGGGTATTCTCA SEQ ID NO:1232 WBCO1OFO4 V1.3_at GGTATTCTCAAAGTCCATTGCCAGC SEQ ID NO:1233 WBCO1OFO4_V1.3_at TAAAGCATTTTCTCCGACTTTCACC SEQ ID NO:1234 WBC010F04 V1.3_at TAGACAGTTTTGTAGATCTCTTTGG SEQ ID NO:1235 Pinin, desmosome associated protein (PlNN)______ __ WBCO12EO7_V1.3 at AATCAGATCTTTGCAGCTTTGAGGG SEQ ID NO:1236 WBC012E07_V1.3_at AATTTGGTTGGCATTTTCTTCATGA SEQ ID NO :1237 WBCO12EO7_V1.3_at CTTTTGTGTTGGCTCTAACTCTGAA SEQ ID NO:1238 WBC0l2EO7_V1.3_at CCTCCTCATCTTTAAACCACGTATT SEQ ID NO:1239 WBCO12EO7_V1.3 at GAGCATCATTCTTTTGTCTCCATGG SEQ ID NO:1240 WBCO12EO7 V1.3 at GTTTCCTCACTTTTATTTGCCTTAG SEQ ID NO:1241 WBCQ12EO7_V1.3_at GTCTCCATGGTTACTTGTGTGATAC SEQ ID NO:1242 WBCO12EO7_V1.3_at GTGGTCTTGTCTTAACTTTTGTGTT SEQ ID NO:1243 WBCO12EO7_V1.3_at GGAGTATCTGTTGCCCATTACTATA SEQ ID NO:1244 WBCO12EO7_V1.3_at TACTGTTTTTTCTAATCTCCCTTGT SEQ ID NO:1245 WBCO12EO7_V1.3_at ITTTAATCTAAGCATTTTCCCCTCCT SEQ ID NO:1246 -369- :P b ~ ~ PROBE SQEC: eune e eNIdentifier, Complement component 5 receptor 1 (C5a ligand) WBC012F07_V1.3_at GAAACAACCAGGAGCCCGTACGGAG SEQ ID NO:1247 WBC012F07_V1.3_at ATATCAGCTGCCTAGAATCCGGACG SEQ ID NO:1248 WBC012F07_V1.3_at ACATCGACACTTCCTTCTAGAGAGA SEQ ID NO:1249 WBC012FO7_V1.3_at GACGCGGTCTAACCCTGTTGAGAAA SEQ ID NO:1250 WBC012F07_V1.3_at GGGAAAATCTGACTTACTCCTTTGT SEQ ID NO:1251 WBC012F07_V1.3_at GGAAGCTACACTGAAGACCGAGGTT SEQ ID NO:1252 WBC012FO7_V1.3_at GGACCTACCCAAGCTTTTGTAAGTG SEQ ID NO:1253 WBC012FO7_V1.3_at GGCAATATTGGTTGGGTCCCTGCAG SEQ ID NO:1254 WBC012FO7_V1.3_at TCCACCCACGGACTTTGAGAAACAA SEQ ID NO:1255 WBC012FO7_V1.3_at TGCGCGAGCAGAGCCCACGAATAGA SEQ ID NO:1256 WBC012FO7_V1.3_at TAGAGAGACCCAACCATTCTTTCCA SEQ ID NO:1257 Soc-2 suppressor of clear homolog (C. elegans) WBC012GO2_V1.3_at CTTGACGCTCAAATTCAGGACTGAA SEQ ID NO:1258 WBC012G02_V1.3_at ATATCCTTTCTTCTTTTTTCCATCT SEQ ID NO:1259 WBC012G02_V1.3_at CAGTATTGTAAATGTGTGCCCCTTA SEQ ID NO:1260 WBC012GO2_V1.3_at CGTATTGCTGCTTGGTTTTCTTTTT SEQ ID NO:1261 WBC012G02_V1.3_at GCGGGTGCATTCTAGATATCATTCT SEQ ID NO:1262 WBC012GO2_V1.3_at GAGACTCACAGAGCGGGTGCATTCT SEQ ID NO:1263 WBC012GO2_V1.3_at GATAGATTTTCTTTTGCTTTACTGC SEQ ID NO:1264 WBC012GO2_V1.3_at GTTATTTTGCTTTTCTTGACGCTCA SEQ ID NO:1265 WBC012G02_V1.3_at GTACTCTTACTTTTGGTAGTGTCAG SEQ ID NO:1266 WBC012G02_V1.3_at GTGTGCCCCTTATACAGTACTCTTA SEQ ID NO:1267 WBC012GO2_V1.3_at TTTTCCATCTACTGTGGCTTTTCAG SEQ ID NO:1268 Sialyltransferase 1 (beta-galactoside alpha-2, 6 sialyltransferase), transcript variant 2 WBC013AO9 V1.3_at AGCTCAGGCCCGATCTGCTTGGGAA SEQ ID NO:1269 WBC013AO9_V1.3_at AGCCCATCTCTCTGAAGGGATTTAT SEQ ID NO:1270 WBC013AO9_V1.3_at AATTCCTGGCTCTCTTTATGTTCTG SEQ ID NO:1271 WBC013AO9_V1.3_at GCCGCTTACTGCTGCGTGAACTAAT SEQ ID NO:1272 WBC013AO9_V1.3_at GAATTGCAGGAAAGCCCATCTCTCT SEQ ID NO:1273 WBC013A09_V1.3_at GAAGGTGGCATTCCATCAGCAGAAG SEQ ID NO:1274 WBCO013A9_V1.3_at GTAGCCATCTATTCAGCCTATATCA SEQ ID NO:1275 WBC013AO9_V1.3_at GTGAACTAATCTTTTCCACCTCTCT SEQ ID NO:1276 WBC013AO9_V1.3_at TGGTGTGGGACCCTGAGACTACACT SEQ ID NO:1277 WBC013A09 V1.3_at TCATGATATCCTCTAATCCTTCCAA SEQ ID NO:1278 WBC013AO9_V1.3_at TTAATTCTGTGCTCTCTCTATATGG SEQ ID NO:1279 Ras GTPase-activating like protein (IQGAP1) WBC013CO3_V1.3_at AGCCTCCACTTTCTCTGATGTGTTG SEQ ID NO:1280 WBC013CO3_V1.3_at AGCCGACGCTGTTACACTTGATATT SEQ ID NO:1281 WBC013CO3 V1.3_at ACTAGGATTTATCTGCAGGGTTGCA SEQ ID NO:1282 -370- Probe Set PROE SE Sece '* 1-", ,';0 __________________________ Identifier WBC013C3_V1.3_at AATCTGTTTTCCCTCATTTCTTTCT SEQ ID NO:1283 WBC013C03_V1.3_at GAATCCTGCCTGAAATAGACTCAAA SEQ ID NO:1284 WBC013C03_V1.3_at GAGCTCCAGTTTTATGGGTTTAGTC SEQ ID NO:1285 WBC013C03_V1.3_at GATGTGTTGGTTCAGTTTTCTTTTA SEQ ID NO:1286 WBC013CO3_V1.3_at GTGCCTTTATTTTTATGAGCTCCAG SEQ ID NO:1287 WBC013CO3_V1.3_at GGGCTTATCTGTATATCTGAACTCT SEQ ID NO:1288 WBC013CO3_V1.3_at TTGAAATCATGCTGCTGAGCCTCCA SEQ ID NO:1289 WBC013C03_V1.3_at TTGCTGCCCACATGGTGCCTTTATT SEQ ID NO:1290 Homo sapiens cDNA FLJ45679 fis, clone ERLTF2001835 WBC013E10_V1.3_at AGAGGATCTCTCTTTTGAAAAGCTA SEQ ID NO:1291 WBC013E1O_V1.3_at AAGAACACTTACAGCTCATATACAG SEQ ID NO:1292 WBC013E1OV1.3_at AAGGAGTTTCCTGTGGTTTCTGCCG SEQ ID NO:1293 WBC013E1O_V1.3_at CGACTATTACTTTCTCTCAAGTGCC SEQ ID NO:1294 WBC013E1O_V1.3_at GAATATGTTCTCCTTTGTAGCCTCT SEQ ID NO:1295 WBCO13E10_V1.3_at GAAAAACACAGCTTAGCCCCTTCCT SEQ ID NO:1296 WBC013E1O_V1.3_at GTAGAATGACACCAAAGCTGCAACT SEQ ID NO:1297 WBC013E1O_V1.3_at GGAAATCAGTCAGTACCATCGTTAA SEQ ID NO:1298 WBC013E1O_V1.3_at TTGTAGCCTCTTGACAAAGCAGGAA SEQ ID NO:1299 WBC013E1OV1.3_at TTGTCCACTGAAACTTTGCTAACGT SEQ ID NO:1300 WBC013E1OV1.3_at TTCCTCTAGCCTTCAGTCAATTTTT SEQ ID NO:1301 WBC013GO8 V1.3 at AGTAAATTGACAGTGGAGCTCCATT SEQ ID NO:1302 WBC013GO8_V1.3_at AGGCATGTACACTTTGATATAGCAG SEQ ID NO:1303 WBC013GO8_V1.3_at AATGCCTGGCCCATGTTACATAGAA SEQ ID NO:1304 WBC013G08_V1.3_at CAGTGGAGCTCCATTTTACAAATGT SEQ ID NO:1305 WBC013GO8_V1.3_at GTTCAGGCATTGCTTTAAACGATGA SEQ ID NO:1306 WBC013GO8 V1.3 at GAATACGTCTGGAATGATCCATTAG SEQ ID NO:1307 WBC013GO8_V1.3_at GATATAGCAGGTTCACCTTAGGAAA SEQ ID NO:1308 WBC013GO8 V1.3_at GTGCAGTCTTACATGTGTACACATA SEQ ID NO:1309 WBC013GO8_V1.3_at GGAAGACTATGTAGCCAGCAAGTAA SEQ ID NO:1310 WBC013G08_V1.3_at TGAATTTAACACATCCATATACTGG SEQ ID NO:1311 WBC013GO8_V1.3_at TAGAGGGTATCAATGCCTGGCCCAT SEQ ID NO:1312 RAB6 interacting protein 1 (RAB6IP1) WBC013HO3_V1.3_at TTCCCAAAGGGACTTCAGCGAGTTG SEQ ID NO:1313 WBC013H03_V1.3_at ACTGAGCCTGCGGTTGCACAGAAGT SEQ ID NO:1314 WBC013HO3_V1.3_at GAAACCAGCTACAGTATGGCCCACT SEQ ID NO:1315 WBC013HO3_V1.3_at GCTTATTTTGAAGCTGGCGCCCTCC SEQ ID NO:1316 WBC013HO3_V1.3_at CCCTCCATTGTGTGTTTTAAGTCTT SEQ ID NO:1317 WBC013HO3_V1.3_at GAAAAGCTTGTCACAGTCTAACTGG SEQ ID NO:1318 WBC013HO3_V1.3_at GAGACGAGGTTGGTGCCGCTTATTT SEQ ID NO:1319 WBC013HO3_V1.3_at GAGAGGAAATGTACACTCACTGTAA SEQ ID NO:1320 WBC013HO3_V1.3_at GATTTGCTTTTTACACACTTTCATG SEQ ID NO:1321 WBC013HO3_V1.3_at GTATTATTTATTTAACCCTCCATTG SEQ ID NO:1322 WBC013H03_V1.3_at GGACCGAGAGAGACTCACCCTGCAG SEQ ID NO:1323 -371- * PobSe aIi: PROBE SEUN' t ~7~ Sequencek'. * **~ ', ~Identifier: RTN4-C (RTN4) WBC14GO8V.3_at ATAGAACTCTTCACGTCGACTGCAT SEQ ID NO: 1324 WBC0l4GO8_V1.3 at AGGTGCACTACCATCTGTTTTCAAC SEQ ID NO: 1325 WBC14G8_V1.3_at AACTTGCCTTTCTGGTATGTTCTAG SEQ ID NO: 1326 WBCO14GO8_V1.3_at AACCCTTTTCACAGTTTGTGCACTG SEQ ID NO: 1327 WBCO14GO8_V1.3_at AAGCTTAGAGACCTTTACCTTCCAG SEQ ID NO:1328 WBCO14GO8_V1.3_at CAAACTCTGACTCTGTGGACT6AAT SEQ ID NO:1329 WBCO14GO8_V1.3_at CCCACAGTGCTTGATCTTTCAGAGA SEQ ID NO: 1330 WBCO14GO8 V1.3 at GACTGCATCGCACAGACTTGCTATA SEQ ID NO: 1331 WBCO14GO8_V1.3_at GACGCCATGCACATAGAACTCTTCA SEQ ID NO:1332 WBC014GO8 V1.3_at GAGAGTCTTTGGTTGTACGTGTGTA SEQ ID NO: 1333 WBCO14GO8_V1.3_at GTTTTCAACGTGAACCGACGCCATG SEQ ID NO:1334 Homno sapiens uRNA; eDNA DKFZp564CO12_______________ WBC014HO6 V1.3_at CTAACATTTGTATGGACCCCTTCAT SEQ ID NO:1335 WBCO14HO6_V1.3_at CAGCAGGACTGATTGCCGGGTGCAA SEQ ID NO:1336 WBCO14HO6_V1.3_at ACCGTTTTTGTCCTAATGCTTCTGT SEQ ID ND: 1337 WBCO14HO6_V1.3 at ACCTCTCTGCCAAACGTGATCTTAA SEQ ID NO:1338 WBCO14HO6_V1.3_at AAATCACACCATCCAGACTGACAAT SEQ ID NO:1339 WBCO14HO6_V1.3_at AACAACTCTCTTTTTGGCAGCAACT SEQ ID NO:1340 WBCO14HO6_VL.3_at AAGCCACACCGTCGTCTGTGAGAAA SEQ ID NO:1341 WBC014HO6_-V1.3_at CTTTGCTCCATTTCATTTTGCCAGA SEQ ID -NO: 1342 WBCO14HO6_V1.3_at GAGAAAGTGCGCCTCCTTAAAGGGT SEQ ID NO:1343 WBCO14HO6_V1.3_at GCTTCTGTTTTATGTGGTGATCGCA SEQ ID NO:1344 WBCO14HO6_V1.3_at TAAAGTGTTCGTTGTGGTGGCCGTC SEQ ID NO:1345 No homology WBCO16A12_V1.3 at ATGCAGATCAGATGGCGTTTCTCCC SEQ ID NO:1346 WBCO16A12_V1.3_at ACGTGTTCAGACTTGTGTTTTCATA SEQ ID NO:1347 WBCO16A12 V1.3_at AAGTATGGGCTGTTTCACGTGTTCA SEQ ID NO: 1348 WBC16A2_V1.3_at GACTATGTACTGTCCACCTGCATTA SEQ ID NO:1349 WBCO16A12_V1.3_at GATTGATTTCCTACTAGTCTTTGAC SEQ ID NO:1350 WBCO16A12_V1.3_at GTTTCTCCCAGCTCAGTGGATTTTC SEQ ID NO:1351 WBC016A12 V1.3_at GGAGCCTGGCTTATTTGATTGATTT SEQ ID NO:1352 WBCO16A12_V1.3_at GGAAGTCCCTGTTCTGACTATGTAC SEQ ID NO:1353 WBCO16A12 V1.3 at TCCCTTCATTCTGGTTTCCATGTGA SEQ ID NO:1354 WBCO16A12_V1.3_at TCACCAACTCCCTTTTGGATTTCAT SEQ ID N'O:1355 WBCO16A12_V1.3_at TAAACAACCATGTCTGCATCTAGGG SEQ ID NO:1356 Homo sapiens gene for JKTBP2, JKTBP1 (alternative splicing).________ WBCO18BO1_V1.3_s_at ATAGCTGCCAATTAGTTTTCTTTGT SEQ ID NO:1357 WBCO18BOlV1.3_s -at AGGCACAACTGTGTCCAACTGTATA SEQ ID NO:1358 WBCO18BO1_Vl.3_s-at AACCCATCTTGCAGGACGACATTGA SEQ ID NO:1359 WBCO18BOl_V1.3_s_at GAAGATTGGTCTTCTGTTGATCTAA SEQ ID NO:1360 WBCO1BBOlV1.3_s at GACTTTCTAGTGTACAAGGCACAC SEQ ID NO:1361 WBCO18BO1_V1.3_s at GACTCAATGTGGATTTGTGTTTATA ISEQ ID NO:1362 -372- **R*O***: kL.U S--- - 2.~ . (ence, - , .. Id6atiier' WBCO18BO1_V1.3_s-at GTTTTTACTTTGTCCTTTGCTATCT SEQ ID NO:1363 WBCO18BO1 V1.3 s at GTGTOCAACTGTATATAGCTGCCAA SEQ I D NO:1364 WBCO18BO1_Vl.3_s-at GGAGATTGCTAAGTAACCCATCTT SEQ I D NO:1365 WBCO18BO1_V1.3 s-at TGCTATCTGTGTTATGACTCAATGT SEQ I D NO:1366 WBCO18BO1_Vl.3_s-at TTTGTCCTTTGCTATCTGTGTTATG SEQ I D NO:1367 Predicted: Mitogen activated protein kinase kinase kinase 1 (MAP3K1) _________________ ________ WBCO18DO5_Vl.3 at GACTTCCAGGGCTTAAGGGCTAACT SEQ ID NO:1368 WBCO18DO5_V1.3_at ATTTGCTGTGTGACTATGATTCCTA SEQ ID NO:1369 WBCO18DO5_Vl.3_at CAAACTGCCTCTAGATGTCCAAATC SEQ ID NO:1370 WBC018D05_V1.3_at CTCAGCTCGCTGGTAATTGTGGTGT SEQ ID NO:1371 WBC018DO5_Vl.3_at GAGGAACCTCAGCTAATCAGTATTA SEQ ID NO:1372 WBCO1BDO5 V1.3_at GTATTACTTGTAGATCCCCATGCCA SEQ ID NO:1373 WBC018DO5_Vl.3_at GTTTGAGTTTGTTTGCAGTTCCCTC SEQ ID NO:1374 WBC018D05 V1.3_at TCAGGTGTCCTATAGATTTTTCTTC SEQ ID NO:1375 WBCO18DO5'V1.3_at TAACGTCTACTGCTGTTTATTCCAG SEQ ID NO:1376 WBC018DO5_Vl.3_at TTTACCCCATCGAACCATTTTATAG SEQ ID NO:1377 WBC018DO5-Vl.3_at TTTATTCCAGTTTCTACTACCTCAG SEQ ID NO:1378 Homo sapiens mRKA; cDKA DKFZp686M2414 _______________ WBCO19BO5 Vl.3_at ATATATGCTGTCTGTTTTGTGTACA SEQ ID NO:1379 WBC019B05 Vl.3_at AACTCACTCTTACAGTAGTCTGCTT SEQ ID NO:1380 WBCO19BO5 V1.3 at AATGTTGTCTTTTAAATACTCCGAT SEQ ID NO:1381 WBCO19BO5_V1.3_at CAAGCCATTTGTGGGAATCCTAAAA SEQ ID NO:1382 WBCO19BO5_V1.3_at CCAGCTGTTTATTTTATTGAGTCCT SEQ ID NO:1383 WBCO19BO5_Vl.3 at GAGTAACAAACTCAGCCTTCTGTAA SEQ ID NO:1384 WBCO19BO5_V1.3 at GAGGATCATCTGACTTTTCACTTAC SEQ ID NO:1385 WBCO19BO5 V1.3 at GTAGTCTGCTTATTTCCAGCTGTTT SEQ ID NO:1386 WBCO19BO5_V1.3_at GTGCTTTATGTACTGTTATCCTATA SEQ ID NO:1387 WBCO19BO5 Vl.3_at TGTAAAAACTCCTTTTCTGCCACAC SEQ ID NO:-1388 WBC01§BO5 V1.3 at TTGGGTTTTCTTTTCAACTCACTCT SQI O18 No homology WBC02OB04_Vl.3-at ATATTGGGCTTTGTCAGTCTTCTGA SEQ ID NO:1390 WBC02OB04_Vl.3-at ATGACAGCTTTTTCTAACGGACAAA SEQ ID NO:1391 WBC02OB04_Vl.3_at AGGATACTCCGTTCTGTAGACACAG SEQ ID NO:1392 WBC02OB04_Vl.3_at ACTCAATTCTGCTGTTGTCGCACAA SEQ ID NO:1393 WBC020B04_V1.3-at CAAATTTCCCTTCTTCTGGCTAATT SEQ ID NO:1394 WBC02OB04_Vl.3-at CTGCCGTCACTGTCATGTTCTAAAT SEQ ID NO:1395 WBC02OB04_V1.3_at GTCAGATCAGACTCCTGTTACAGCT SEQ ID NO:1396 WBC02OB04_V1.3_at GGATGTTTTATCTGAACGCCTGCTC SEQ ID NO:1397 WBC02OB04_VI.3_at TGGCTAATTCCTACACTTTTTCTCA SEQ ID NO:1398 WBC02OB04_V1.3_at TAAGGTCCACCACTTGTTCTTTGTT SEQ ID NO:1399 WBC02OB04_V1.3_at TAAGGCTCTCTAACACTGGCTGCT SEQ ID NO:1400 Hypothetical protein FLJ20481__________________ -373- * ~ e am.. -**PROBEEUNE~ ~. Sequence Identifier' WBC021B08_Vl.3_at ATAGCTCAGGGCGATTCTGTGTCGT SEQ ID NO: 1401 WBCO2lBO8_V1.3_at AACATACTTAGACCTCCAGACGAGC SEQ ID NO:1402 WBCO21BO8_V1.3_at AGCATTATCAACACCTAGAGCTTAA SEQ ID NO: 1403 WBCO21B08_V1.3_at AACGCGTGGCTCTTTCTTGAAATTG SEQ ID NO:1404 WBCO21BOBV1. 3_at AAAGTTTTGCCCTGAAGCATCCAGA SEQ ID NO:1405 WBCO2lBO8 V1.3 at AATCGTGAAGAGAGCGCCTCAGACA SEQ ID NO:1406 WBCO21BO8_V1.3 at GCAACTCCCTCATTCACAAGTAATA SEQ ID N'O:1407 WBCO21BO8 Vl.3 at GACAGTACATTTTCCCAGCAAAGTG SEQ ID NO: 1408 WBC021B08_Vl.3_at GAGCCATGTGTTTTCACTGCCAAAA SEQ ID NO:1409 WBCO21BO8_V1.3 at GGTCTCACTTAGTTATTGATCAGCA SEQ ID NO:1410 WBCO21BO8_V1.3_at TATTGTGCTGTCCTGATTGGTTTAC SEQ ID NO:1411 No homology WBCO21DO1_Vl.3 at CGTTCTCCGGTCTGTAGCGATTTGA SEQ ID NO: 1412 WBC021D0l_V1.3_a t AAGAAGTAAGCAGCACCCGTTCTCC SEQ ID NO:1413 WBCO21DO1 Vl.3_at AGGCGCCTGTGCCAGATTATAATCA SEQ ID NO: 1414 WBCO21DO1_V1.3_at AGTGACACACTTAGCTTTCTTTCTG SEQ ID NO:1415 WBCO21DO1_V1.3_at AAGCTCACTCTTTCATGTTGGATGG SEQ ID NO:1416 WBCO21DO1_V1.3 at CTGCCCTCCATCTTAACTTTTATTA SEQ ID NO:1417 WBCO2lDO1_-V1.3_at GAAACTTGTCCTTATTCATTGTTGT SEQ ID NO:1418 WBC021D01_V1.3_at GGATCACAAATCGTTCATAGACCAT SEQ ID NO: 1419 WBCO2lDO1_VI.3 at TAATCAACACATCGCTTCCTTTATC SEQ ID NO:1420 WBCO21DO1_V1.3_at TTTCACACAAGTTACAACTGCCCTC SEQ ID NO:1421 WBCO21D0l_V1.3_at TTTCTTTCTGGCACAAGCTCACTCT SEQ ID NO:1422 Toll-like receptor 8 (TLR8) _________ WBCO22BO5_V1.3 at TCCCAAACTTTCTACGATGCTTACG SEQ ID NO:1423 WBCO22BO5_-V1.3 at AAAGACGCCTCTGTTACGGACTGGG SEQ ID NO:1424 WBCO22BO5_V1.3 at ATTCCCAGTATTTGCGGCTGCGGCA SEQ ID NO:1425 WBCO22BO5_V1.3_at ATTGGGACCCGGGATTAGCCATCAT SEQ ID NO:1426 WBCO22BO5_V1.3 at AAAAGGCTACAGGTCTCTTTCCACA SEQ ID NO: 1427 WBCO22BO5 Vl.3 at AAACAGCATTCTACTTGGCCTTGCA SEQ ID NO: 1428 WBCO22BO5_-V1.3 at GAGCCAGTGTTACAGCATTCCCAGT SEQ ID NO:1429 WBCO22BO5 V1.3 at GATGCTTPACGTTTCTTATGACACCA SEQ ID NO:1430 WBC022BO5 V1.3 at GATTGTATTTATTCTGCTGGAGCCA SEQ ID NO:1431 WBCO22BO5_V1.3_At TGATAAATGAGCTGCGCTTCCACCT SEQ ID NO:1432 WBC022B05_V1.3_at TTAGCCATCATCGATAACCTCATGC SEQ ID NO:1433 Immunoglobulin superfamily, member 6 variant WBC022B06_V1.3_at AATAAGCCACAACCGACTCTAGATG SEQ ID NO:1434 WBCO22BO6 V1.3 at AAAATCACTTACATCATGCCGCCAA SEQ ID NO:1435 WBC022B06_-V1.3 at AAGTGCCCACATTTGAGTCAGCGAA SEQ ID NO:1436 WBCO22BO6_V1..3_at AAGGCGCCTCTGCAATACTGATTTT SEQ ID NO:1437 WBC022B06_V1.3_at AATCATCTTGAAAACTACCTTGGAG SEQ ID 14:1438 WBC022B06_V1.3 at CAAACGATTCCTCTGGTATTGCCAT SEQ ID NO:1439 WBCO22BO6_V1.3_at CTCTAGATGTCAGTGTTGTGCCAAA SEQ ID NO:1440 WBC022B06_V1.3 at GTGATGGGCCAGTCAGACTAAGCTG ISEQ ID NO:1441 -374- Pz4be set-Name Q" >eqPROB WBCO22BO6 V1.3 at GGTATAGTGCACATTTTCCTGCCAG SEQ ID NO:1442 WBCO22BO6_-V1.3_at TTTCCTGCCAGGGTATACAAAATCA SEQ I D NO:1443 WBCO22BO6 V1.3 at TAGGAGTGGGCAAGGCACCGTCCTT SEQ I D N0:1444 Phosphogluconate dehydrogenase_________________ WBCO22FO8_V1.3_at ATGCCTAATCAGACTCCTTGTGTTA SEQ I D 1.1:1445 WBCO22FO8_V1.3_at ATGCAGGTGAATTCCCTTTTTCCTC SEQ I D NO:1446 WBCO22FO8_V1.3_at AGGCAGOAGCTCCTATCACATAGAT SEQ I D 140:1447 WBC022FQ8_V1.3_at AGTGTGTCATCCTCTTCGTACAATG SEQ I D NO:1448 WBCO22FO8_V1.3_at ACCCGGACAGTTTATCCACACTAAT SEQ I D 1.1:1449 WBCO22FQ8_V1.3_at ACTGCTCTTTCCTTCTATGATGGAT SEQ ID 140:1450 WECO22FOBV1.3_at CTTGTCTCTTGGGACTGACCAGGAA SEQ I D 1.1:145. WBCO22FO8_V1.3 at CTATTTTCTGCTCACATCTCTTAAA SEQ I D 140:1452 WBCO22FO8_-V1.3_at GATGGCGCAAACCAGCTGCCTGAAG SEQ ID NO:1453 WBCO22FO8_V1.3_at GTATGAACTCTTAGCCAAACCCGGA SEQ ID 140:1454 WBCO22FO8 V1.3 at TAGACCAGGACATTCCATTTGCCAC SEQ ID NO:1455 Adducin 3 (gamma) (ADD3), transcript variant 2 _______ WBCO24BO5 -V1.3 at ATGAACCTCTGTGTCCTGTGGAAAA SEQ ID 140:1456 WBC024B05_V1.3 at ATGAGCCAATGAACCTCTGTGTCCT SEQ ID 140:1457 WBC024B05_V1.3_at AGTGAACTATTTGCACCTTTTGCTA SEQ ID NO:1458 WBCQ24BO5 V1.3 at CACCTTTTGCTAATGCCTCTATTTA SEQ ID NO:1459 WBCO24BO5 V1.3_at CAGTGTTTTAATCTCTTAGTGGAAA SEQ ID NO:1460 WBC024B05_-V1.3_-at CTGGTTCTGTTTGGCGTATGTGTAT SEQ ID 1.01461 WBC024B05 V1.3_at GCCTCTATTTACTTGCTTTGGCATA SEQ ID NO:1462 WBCO24BO5_V1.3_at GATCTCACTAACTACTGGAATCAGT SEQ ID 140:1463 WBC024B05_V1.3 at GTAACCTGTGAACTATGCTTTTCCA SEQ ID NO:1464 WBCQ24BO5 V1.3 at GGAAACTCTCAGTTGCTTAATTCTG SEQ ID NO:1465 WBCO24BO5_V1.3_at GGAAATTTdATTTTAGATCTCACTA SEQ ID 140:1466 No homology WBCO24C.1 V1.3 at ATGTCTATTTCATGCCTACGCTTAA SEQ ID 140:1467 WBCO24C11 .V1.3_at AGACCATACAGTTTTATCCCACAAG SEQ ID 140:1468 WBCQ24C11_V1.3 at CCTGCCTCGTGGTTTCTCTAGAAAA SEQ ID 140:1469 WBCO24C11 V1.3 at GTTTACCTGGGCTTGGAATTCTAGA SEQ ID 140:1470 WBC024C1_V1.3_at GATCTGACTCTGAAATTTCCTTTAG SEQ ID 140:1471 WBCO24C11 V1.3_at GTTTTTCACTCTAATCTGCATTCCC SEQ ID 1.1:1472 WBCO24C11_V1.3_at TTTTCCCCAGGCTGCTTGTAAGATC SEQ ID 140:1473 WBCO24C11_V1.3_at TAGTCCTTTCTTCTGGTTAACTAAT SEQ I D 1.1:1474 WBCO24C11_V1.3 at TCACATCATATATTGCCTCTTTCCT SEQ ID 140:1475 WBCO24C11_V1.3_at TAGTTATCCTGTCTTTTTTCCCCAG SEQ ID NO:1476 WBCQ24C11_V1.3_at TATAAGTGGTAGACACCTCCTGCCT SEQ ID 140:1477 No homology WBC024C12 V1.3 at AGGCCACATATCTCCGTCTTTTTAA SEQ ID 140:1478 WBCO24C12_V1.3_at ATATGCTTTCATTTCTCTTGTGTAA SEQ ID 140:1479 WBC024C12 V1.3_at AAATACGCCACAATTTGTCCACTCA SEQ ID 140:1480 WBCO24C12_V1.3_at 1AAAACTCCTTGGGTGTGATCACGCA SEQ ID 140:148 1 -375- ProbW, -SE _TPROBE.. Sequencb~.. WBC024C12_V1.3 at AATGTTTTCTCATATCCCTGTTATA SEQ ID NO:1482 WBCO24C12_VI.3_at GCATTTATTTGTGCTAACCTCTGAA SEQ ID NO:1483 WBC024C12_Vl.3_at GTATGTACTCTTTTGGGTCTGGTTC SEQ ID NO:1484 WBCO24Cl2_V1.3_at GTCTGGTTCATCCATGTTGTAGCAT SEQ ID NO:1485 WBCO24Cl2 Vl.3_at GTGAACCTACTTAACAATCCTCGTC SEQ ID NO:1486 WBC024C12_V1.3_at TATTCACTGTTGTCTGTTCTTCTAG SEQ ID NO:1487 WBC024Cl2_V1.3_at TTAGATACCAACCTCCAAGATGCCA SEQ ID NO:1488 No homology WBC024F08_V1.3_at ATGTGTGTCTCTATGTACCCAAGCC SEQ ID NO:1489 WBCO24FO8_V1.3_at AGCTCTGCAAGTCACTTACCTGAAG SEQ ID NO:1490 WBCO24FO8_V1.3_at AGACTCAGGGATGCTGTTTCCAGCT SEQ ID NO:1491 WBCO24FO8_V1.3_at AGCGTGTGTCTACATGTGTGTCTCT SEQ ID NO:1492 WBCO24FQ8_V1.3_at AAGCACAGTGTCTCTCGAATTTCGG SEQ ID NO:1493 WBCO24FO8_Vl.3_at GAGAGGCGAGCATCTGGCTGTACTT SEQ ID NO: 1494 WBC024FO8_V1.3_at GTACCCTCCTCACATTTTTGCATAT SEQ ID NO:1495 WBCO24FOB_V1.3_at GGTGGCCACCTGCATGAGTGTATTA SEQ ID NO: 1496 WBC024FOB _Vl.3_at GGATGCATTCTCTTGTTTTGCTTGA SEQ ID NO: 1497 WBCO24FO8 V1.3_at TGAGTCCTGTGAGATGCCCTTGTTA SEQ ID NO:1498 WBCO24FO8_V1.3_at TCTGGTTCTCTCTCTCAGGMATAAG SEQ ID NO:1499 Migration-inducing gene 10 protein WBC026E02 V1.3_at AGGTGGTGCCAGTTTAGAGCTCCTG SEQ ID NO: 1500 WBCO26EO2_V1.3_at ACTGCCACTTGCTGTGCCAAATGGA SEQ ID NO:1501 WBC026E02_-V1.3_at AAACAGTTGCACAGCATCTCAGCTC SEQ ID NO:1502 WBC026EO2_V1.3_at CAATGTTTAGTACTTTCCTGCCTTT SEQ ID NO:1503 WBCO26EO2_-V1.3_-at GCTTTGTCATTGTTTCACTACTCAG SEQ ID NO:1504 WBCO26EO2_V1.3_at GAGCTGTTAGCCTAGTTCTCTTTTT SEQ ID NO:1505 WBCO26EO2_V1.3_at GAGATGCAGCACCAGGAACCCTTAA SEQ ID NO:1506 WB0026E02 Vl.3_at TGTGCGCAGCCCTTAAGTCAACTTA SEQ ID NO:1507 WBCO26EO2_Vl.3 at TAAGTCAACTTAGCGCTTTCCACAT SEQ ID NO:1508 WBCO26EO2_V1.3_at TCAGGATCCCATTTGCATTTCTTAG SEQ ID NO:1509 WBCO26EO2_V1.3_at TACTGCACTCTGGATTTGCCTACAT SEQ ID NO:1510 No homology WBC027DO7_V1.3 at ATTTTTGTCTTTCACTCTTTTCCTG SEQ ID NO:1511 WBCO27DO7_-V1.3 at ATCCCTGATAATTTTCCTCACTTGG SEQ ID NO:1512 WBCO27DO7_-V1.3_-at CACTTGGTTGTTTGCTCTGTCTGAA SEQ ID NO:1513 WBCO27DO7_-V1.3_-at GATTAACTCTGTCTTTTAGCTGGTA SEQ ID t1O:1514 WBC027D07 Vl.3 at GTAAGCCTCTTTATCATTCTCTAAT SEQ ID NO:1515 WBC027D07_-V1.3_at GTGGGTTTCCTCTAGATAGCATATA SEQ ID NO:1516 WBCO27DO7_V1.3_at GGCTCTTGTTTTTTGATTCACTCTG SEQ ID NO:1517 WBCO27DO7_Vl.3_at TCCAGCTTTCTTTTGCCTAGTGTTA SEQ ID NO:1518 WBC027D07_V1.3_at TATACTGTTTTCTACTGGTTGCCCT SEQ ID NO:1519 WBCO27DO7_V1.3 at TAATGCCCTTCTTTATCCCTGATAA SEQ ID NO:1520 WBCO27DO7 V1.3_at TATATTTTTCTCCATCCCTTTACTT SEQ ID NO:1521 No homology WBC27EO7V.3_at IATAGGGTGGTGGACCTTATGGCCCA = SEQ I D NO:15221 -376- PrNb S~~aro:; 'a:-=UKCI Sequ~ne WBC027E07_V1.3 at ATATTGAGAGTCTCCTGACCTCCAC SEQ I D NO:1523 WBC027E07_Vl.3_at AGAAAGGCCCTCAGCTGCTGGGAAT SEQ ID NO:1524 WBCO27EO7_V1.3_at ACTTTGTCAAGCTCATTTCCTGGTA SEQ ID NO:1525 WBC027E07_Vl.3_at GCTGGGAATGCTTGTCCCAACTTGA SEQ ID NO:1526 WBCO27EO7_V1.3 at GAGACTAGTTCTCTCGTGACACCCA SEQ I D NO:1527 WBCO27EO7_1.3_at GGCCCACATGGCCTCCAAGGAGTAA SEQ I D NO:1528 WBCO27EO7 V1.3_at GGAGCCCTACCTTGTCATGTACCAT SEQ I D NO:1529 WBCO27EO7 V1.3 at GGACCACCAATCACCCAGCAAGAGA SEQ I D NO:1530 WBCO27EO7 V1.3_at TGACCTCCACAGTTTCCATCTCAGA SEQ ID NO:1531 WBCO27EO7_V1.3_at TTGCCCTCAACGACCACTTTGTCAA SEQ ID NO:1532 Ras homolog gene family, member A WBC028C01_V1.3_at AGTGGGCATCCAGTTTTTTGAAAAT SEQ I D NO:1533 WBCO28CO1_V1.3_at AGTGTATGATTACTGGCCTTTTCCA SEQ I D NO:1534 WBCO28001_V1.3_at AGATTTCATCGCATAGCTCTGGAGT SEQ I D NO:1535 WBCO28CO1_V1.3 at ACACCAGGCGCTAATTCAAGGAATT SEQ ID NO:1536 WBCO28CO1_V1.3_at AAAGGCCCAAGTCCGTGAGCAGCTA SEQ ID NO:1537 WBCO28CO2._V1.3_at AACATGTCCTGACTGTCATCTGTCA SEQ ID NO:1538 WBC028001_V1.3_at GAAGTCATCTTGCTACGAGTATTTA SEQ I D NO:1539 WBCO28CO1 V1.3 at GAGCTTTACTCCTTAACAGATTTCA SEQ ID NO:1540 WBC028COlV1.3_at GTGAGTCACCACTTCAGAGCTTTAC SEQ ID NO:1541 WBCO28CO1_V1.3 at TCATCTGTCAGCTGCAAGGTACTCT SEQ ID NO:1542 WBCO28CO1_V1.3 at TATTAATGATGTCCAACCCACCTGA SEQ ID NO:1543 No homology WBC028D09_V1.3_at AGGAGTCGGCGCACTGGGTCACCCA SEQ ID NO:1544 WBCO28DO9_V1.3 at ATGAAAAGGTCCATCGCCGACAGCG SEQ ID NO:1545 WBCO28DO9_V1.3_at AGAAGAAGACCAACTCTGCTCCCAA SEQ ID 1NO:1546 WBCO28D9_Vl.3_at AAGCCGGCCTTGATTCTAGAGAGAA. SEQ I D NO:1547 WBCO28DO9_Vl.3_at GAAGCCTCCGTGTGGAGCCATGAAA SEQ ID NO:1548 WBCO28DO9_V1.3_at GAAGCTCTTCTGGAAAAGTCGGGAA SEQ I D NO:1549 WBC02BD09_Vl.3_at GAAAGCTCTGTTGGCTGCACTTTTT SEQ I D NO:1550 WBCO2BDO9 V1.3_at GAGTCGGTCTCAAAGCCAGATGTCA .SEQ I D NO:1551 WBCO28009_-V1.3_at GGGCCTCTGTTTGACGGCATTAGAA. SEQ I D NO:1552 WBCO28DO9 -V1.3_at TAAGTCTCTGTTCACAACTCACAGC SEQ I D NO:1553 WBC028D09_Vl.3_at TTAGAAAGTTGTCCGCCGAGCTGGC SEQ I D NO:1554 Homo sapiens cDNA FLJ13038 fis, clone NT2RP3001272, weakly similar to Mus musculus mRNA for macrophage actin associated-tyrosine WBC028E07_V1.3_prtein TGGCTCTTGCC SQI O15 WBC028E07_V1.3 at AGACTGGGTCTTGCTTATGACAGA SEQ ID NO:1556 WBCO28EO7_V1.3_at AAATATTTTCCTGACCTGCTCTGTG SEQ ID NO:1557 WBCO28EO7_V1.3_at ICAGCACTGGCACTTATTTGGTATGT ISEQ ID NO: 1558 WBCO28EO7_V1.3_at IGAAGATTGATTATTCCCTCCTTTTA ISEQ ID NO:1559 -377- Probe. SQtMm 'E ''M. B SE ~*sequ nce:. -' ~Identifier.* WBC28EO7Vl.3_at GTGTTAATCTTACCCTTTCTCAAAT SEQ ID NO:1560 WBCO2SEO7 Vl.3 at GGAGACCGTGTACTTTTTGTGCAAC SEQ ID NO:1561 WBCO28EO7_Vl.3_at TGCTCTGTGCATAGCTTACCCAGAA SEQ ID NO:1562 WBCO2BEO7_Vl.3_at TTTATTGTTGGCACTTCCTCAGGGA SEQ ID NO:1563 WBCO28EO7 Vl.3_at TTTCTCCCTATTGGTCAGTGTGATT SEQ ID NO:1564 WBC02BE07_Vl.3_at TTGACTTCCCCAAACTGAACAGGCT SEQ ID NO:1565 No homology WBCO28FO5_V1.3_at AGATGTCTTCCTTCTCAATTTTGAG SEQ ID NO:1566 WBC028F05_-Vl.3_at AAAGATCTTTTGGTTTCTCTGTCAA SEQ ID NO:1567 WBCO28FO5_Vl.3_at AAACTGTCCTTTCCATTAGCATTCT SEQ ID NO: 1568 WBCO28FO5 V1.3_at AAGAATTTGTCCTAGGGCTGCTTTC SEQ ID NO: 1569 WBC028F05 Vl.3_at CAGCCTTTACAGACCTTGTTTTCAG SEQ ID NO:1570 WBCO28FO5_Vl.3_at GTTTTTTCCCCTCATACATTCTAGA SEQ ID NO:1571 WBCO28FO5_Vl.3_at GTTCAGTTCGTTTCCATAGTAGCCA SEQ ID NO: 1572 WBCO28FO5_Vl.3_at GTAGCTTTAATCACATCTCTTCCTT SEQ ID NO: 1573 WBCO2BFO5_Vl.3 at TCTTCCTTAGAAGTCTCAGCCTTTA SEQ ID NO: 1574 WBCO28FO5_V1.3_at TAGGACCCATTTATCTTTCTTACCA SEQ ID NO:1575 WBCO28FO5_Vl.3_at TTGCCTGAGAACATTCATCCTGCTT SEQ ID NO: 1576 No homology WBCO30004_V1.3 at ATGCGCACATTTACTAGCACCTACT SEQ ID NO: 1577 WBC03OC04_Vl.3-at ATGGACTTCGCTGCATTGTATGAGA SEQ ID N'O:1578 WBCO3OCO4.Vl.3_at ATGTGCTGTGTGCTCTGTGTACCCT SEQ ID NO:1579 WBCO3OCO4_-V1.3 at AGTTGTCTGGCCCAAAGCATCAGCA SEQ ID NO:1580 WBCO3OCO4 V1.3 at GAGTTCGATTCCCATCTGAAACGAC SEQ ID NO:1581 WBC03OC04_Vl.3_at GAGACATTTTCCGTTGTCACAACTT SEQ ID NO: 1582 WBCO3OCO4_V1.3_at GAGAGGTCACCGATGCTGCTAAACA SEQ ID NO: 1583 WBCO3OCO4_-V1.3_-at GTGTGGCCTTAGTGACCAATCAGTC SEQ ID NO: 1584 WBCO30O4 -V1.3_-at TG:TGTACCCTCAGATCACGTGAACT SEQ ID NO:1585 WBC03OC04_Vl.3_at TACTGAGGGCTTACCATGTGCTGTG SEQ ID NO: 1586 WBC03OC04_Vl.3_at TTCACCCCTCGGAACATCGATGATG SEQ ID NO: 1587 Putative membrane protein (GENX-3745 gene) WBCO3ODO2 Vl.3 at AAGAAAGTTCCACCATAATGACCCT SEQ ID NO: 1588 WBC03OD02_VI.3-at CTATGGTCTTTATTTCTTGTGGTGA SEQ ID NO:1589 WBC03OD02_Vl.3-at CCTAATTCCCTTCCTGATGTGTATT SEQ ID NO:1590 WBC03OD02_Vl.3-at GTTGTTTAACGTCTTCTGATTCAGT SEQ ID NO:1591 WBCO3ODO2 V1.3 at GTCAGTAGGATTTTTGGTACCACCA SEQ ID NO: 1592 WBCQ3ODD2_V1.3_at GTAAAATTCTCCAACTGCTATCTAT SEQ ID NO:1593 WBC03OD02_Vl.3_at GGTGAAACGATGTGCCTTTCCTTGC SEQ ID NO:1594 WBC03OD02_Vl.3-at TGGCTGGTCATTAACTTCCAACTAT SEQ ID NO: 1595 WBCO3ODO2 Vl.3 at TCCTTCACACATCAGGCTCATTAAG SEQ ID NO:1596 WBC03OD02_Vl.3_at TAATGACCCTCCCAAGCTAGGAAAA SEQ ID NO:1597 WBC030D02_Vl.3_at TTTGGATTTTGCTTOTTCCTTCACA SEQ ID NO:1598 DDHD domain containing WBC032B05_V1.3_at ATGTCTCTGCATGTTATCACGGAAT ISEQ ID NO: 1599 -378- PROBE SEQENC -+-' equ.o __________________________I Identikier WBCO32BO5_V1.3_at GCAACATTCAAMACCGCCTTTTCAA SEQ ID NO:1600 WBC032B05_V1.3_at AAATATGTCTGCTTCCCTTTTTTCA SEQ ID N'O:1601 WBC032BO5_V1.3_at GCTTTCAGTTCATTATTTCATCCAT SEQ ID NO:1602 WBCO32BO5_V1.3_at GCAGCTTTATTTCAGCAAGTACTAA SEQ ID NO:1603 WBCO32BO5_-V1.3_-at GAAGAGTCCTTTTCACCTAAGAGTG SEQ ID NO:1604 WBC032B05_V1.3_at GATATTCTGCATTACTGGACGGATA SEQ ID N'O:1605 WBCO32BQ5_V1.3_at GGTGGTATGACACTCAAATGCCTAC SEQ ID NO:1606 WBCO32BO5_V1.3_at GGATTCATTCTTAACCACTACGGTG SEQ ID NO:1607 WBC032B05_V1.3_at GGACGGATATTTTGCTTTCAGTTCA SEQ ID NO:1608 WBCO32BO5 V1.3_at TACAGTACTCTTGTTTCCATGTCTC SEQ ID NO:1609 WBCO32B11_V1.3_at ATTTGGGTCTATGCTATGTTATTAA SEQ ID NO:1610 WBCO32B11J._V1.3_at ATCGGTACGTTGGAAACTGTGCAAA SEQ ID NO:1611 WBCO32B1_V1.3_at ACTTTTGTGCAATATCTGTCTGATT SEQ ID NO:1612 WBCOS2B11_V1.3 at AACTATTCTTGATTCTGTCTGTGCC SEQ ID 140:1613 WBCO32B11_V1.3_at AAGATGTTTCTATTTTGGGCAGCAT SEQ ID N0:1614 WBCO32B11_V1.3_at CTTTGTGTTTTATTTTCTGTCCTAT SEQ ID 140:1615 WBCO32BI1 V1.3 at GAAGATATTCCATTTCTTTGTGTTT SEQ ID 140:1616 WBCO32B11_V1 .3_at GATTCTGTCTGTGCCTTTATATTTT SEQ ID 140:1617 WBC032B1l1_VIA.3 at GTATGGAATTACTGACTTTTGTGCA SEQ ID 140:1618 WBCO32B11_V1.3_at GGCACTTAGGAACATATCGGTACGT SEQ ID N0:1619 WBCO32B11_V1.3_at TTAGAGTCTATTTCCCATAATTTGG SEQ ID 140:1620 Glycerol kinase (GK) WBC032GO5_Vl.3 at ATGAACCGCGACTGTGGGATTCCAC SEQ ID N0:1621 WBCO32GO5_V1.3_at AAACAACGGCTCTGGGAGCTGCCAT SEQ ID 140:1622 WBC032GO5 1.3_at GCTGACATTCTGTACATCCCAGTAG SEQ ID 140:1623 WBC032G05_V1.3 at GAATCCAGTGGTTGTCTCTAAATGT SEQ ID N0:1624 WBCO32GQ5_V1.3_at GAACCCGAGGATTTGTCAGCTGTCA SEQ ID NO:1625 W.BCO32GO5 V1.3 at GTAGTGAAGCCCTCGATGCCTGAAA SEQ ID N0:1626 WBCO32GO5_V1.3_at GATTCCACTCAGTCATTTGCAGGTA SEQ ID NO:1627 WBC032G05_V1.3_at GTTGGGTTACAACTCAGTCTTCGGA SEQ ID N0:1628 WBCO32GO5_V1.3_at GTGGGCTCACACAGTTCACCAATAA SEQ ID 140:1629 WBCO32GO5_1.3_at TGCCATATTGCTTTTGCCGCATTAG SEQ ID 140:1630 WBCb32GO5_Vl.3_at TAGPAGCTGTCTGTTTCCAAACCCG SEQ ID 140:1631 SelenoproteiLn P WBCO37F12_V1.3_at ATCTTGATTTTTACTACCACATATG SEQ ID NO:1632 WBC037F12_Vl.3 at ATCTTGTTTTCTTTATCTAGCATCG SEQ ID 140:1633 WB0037F12 V1.3 at AATATCCACTTATACGTACATCTAA SEQ ID 140:1634 WBCO37F12 -V1.3_at CCTGAACTCCTTTATGGTTAATACT SEQ ID NO0:1635 WBCO37F12_V1.3_at GCTATCTTTGTCTTTTTCATCTTAT SEQ ID NO:1636 WBCO37F12_V1.3_at GAATGCAATACACAGTTGGCCAAGT SEQ ID 140:1637 W8C037F12_V1.3_at GAATATTTTGCTATGACTACAGTTT SEQ ID 140:1638 WBC037F12_V1.3_at GAATGTTGTCTATCTCTTGATTGCT SEQ ID 140:1639 WBCO37F12_-V1.3_at GAAATGTGAGAGTGCCCCTTGAAAG SEQ ID 140:1640 WBC037Fl2_V1.3_at TCTAGCATCGTATCGCACTTTGAAA SEQ ID 140:1641 WBCO37F12_V1.3_at TAAGTCCTATAAACCTGAACTCCTT ISEQ ID 140:1642 -379- NamC44 -c sequence __________________ -. ~ -~~y2Identifier No Homology WBCO38G1J._V1.3 at ATCTGTGGCGGATGTTTCTTCTCTG SEQ ID NO:1643 WBCO38G1lVl.3_at AGGAGTTCTCCTGAGCTCAGCCGAG SEQ ID NO1:1644 WBCO38Gl1_Vl.3_at AGCAGTTCTTCCTGAACGGCTTTGA SEQ ID NO:1645 WBCO38GlV1.3_at AGACTGACAGCTGACTCCCAGGAGT SEQ ID NO:1646 WBC038G1lVl.3 at ACGTGCATGTGTCTTCCAGGAGCAT SEQ ID NO:1647 WBC038G11 Vl.3_at AAACAAGCGACATCAGCACCTGGGA SEQ ID 1.1:1648 WBCO38GlV1.3_at AAGGAAGGGCTCTGCCTGAGCAGTT SEQ ID NO:1649 WBCO38GllVl.3_at GAACTTGGTCGCATTTGGTCTGAAA SEQ ID NO:1650 WBC038G11_Vl .3_at GAAGGAGTTCCCTGATCGGCTACAG SEQ ID NO:1651 WBC038G11_V1.3_at GTGAACTGCCTGTTGAACTTGGTCG SEQ ID NO:1652 WBCO38G11_Vl.3_at GGAGCATTGCACGTTGCCTGTAGAA SEQ ID NO: 1653 Leu-8 pan leukocyte antigen ________________ WBCO39Fl2_V1.3_at ACATGCACCTTCAACTGCTCAGAAG SEQ ID NO:1654 WBCO39F12_Vl.3_at AAACATTTGGCTGATTTTTGCTTTT SEQ ID NO1:1655 WBC039F12_-V1.3_-at GCAGGAtACCAAGCTCTATGTTTTA SEQ ID 140:1656 WBC039F12_V1-.3 at GATCATCAGGAATCTGGTCCAGCAC SEQ ID NO:1657 WBCO39F12_Vl.3 at GTTGGCATTTATCATTTGGCTGGCA SEQ ID NO: 1658 WBC039F12_Vl.3_at GTTTTATAGACATCAGTCCCTGGAG SEQ ID NO: 1659 WBC039F12 V1.3_at GTGAAGCAGCCCAGTACATACTTTC SEQ ID NO:1660 WBCO39F12_-V1.3_-at GTCATGGTTACTGCATTATCTGGGT SEQ ID NO1:1661 WBCO39F12_Vl.3_at GGTCCAGCACTAGTCCAATGTGTCA SEQ ID NO: 1662 WBC039F12_V1.3_at TGGACAGGAGTTTCACGGCGATCAA SEQ ID NO: 1663 WBC039F12 Vl.3_at TCATCCCTGTGGCAGTCATGGTTAC SEQ ID NO:1664 WBC040E12_Vl.3_at AAATCATCATAACTCAACTCCTACG SEQ ID 140:1665 WBC04OE12_V1.3_at AACTTTGTGTCAGCGATACCCTTTA SEQ ID 140:1666 WBCO4OE12_Vl.3_at AACTATTATCTCATCCTCTTTTTCG SEQ ID 140:1667 WBC04OE12-Vl.3_at AATACAGGGTTGGTGCTCTCATCTA SEQ ID NO:1668 WBC040E12_V1.3-at GAAGTACTTCGTGGGCTATCTGGGA SEQ ID NO:1669 WBC04OE12_Vl.3_at GAAACGCATCATACTGTTCCTGTTC SEQ ID NO: 1670 WBC040E12_Vl.3_at GAGTTAACCTTGCTTTTCCTGGAAG SEQ ID NO1:1671 WBC04OE12_Vl.3-at GATCCATTCTGTGTGTTTCTTGACT SEQ ID NO:1672 WBC04OE12_Vl.3_at TGGGCTTCGCGTCTTGAGTTAACCT SEQ ID NO: 1673 WBC040E12_Vl.3_at TACGGTCCTCTTTAGATTGCTGTAA SEQ ID 140:1674 WBCO4OE12_V1.3_at TTGACTTACCCTGCTTTCTGAAGAT SEQ ID NO: 1675 WBC04lB04_V1.3_at ATAAAGCCCTGGAGGGCCCTGAGGC SEQ ID NO:1676 WBCO4lBO4_V1.3_at AGAATGGGACCATTTCTCTGTGAAT SEQ ID NO:1677 WBCO41BO4_Vl.3 at ACCACTTTCCTATTTCACCTGATTT SEQ ID 140:1678 WBC041BO4_V1.3_at AAGGGTACATTTCTCCTATGGCCGA SEQ ID NO1:1679 WBC041BO4_V1.3_at CTATGGCCGATTTCAGGAATTTCAA SEQ ID 140:1680 WBC041BO4_Vl.3_at CCTGAGGCTCACTGCTGACTGAGAA SEQ ID 1.1:1681 WBCO41BO4_Vl.3_at GACTGAGAACTCTGTGGAACATGAT SEQ ID NO:1682 WBCO4lBO4_V1.3_at IGAGAATCCTTCAGTTCATTCACAAA ISEQ ID NO:1683 -380- P- j :.RBE'E Sequence ~ ... ~.. Identifier i WBCO41BO4_V1.3 at GTGTTAACCATGAAAGTACTCGAAG SEQ ID NO1:1684 WBCO41BO4_V1.3_at GGAACATGATCCTAGGCACTGAAGT SEQ ID N.01685 WBC041BO 4 V1.3 at GGCACTGAAGTATCGACCACTTTCC SEQ ID NO1:1686 ARP3 actin-related protein 3 homolog (yeast) WBC41BO5V1.3_at ATTTATCGGTATGTAGATAGCTCTA SEQ ID NO; 1687 WBCO41BO5. V1.3 at ACACTTCTAAGTGGGCAATGCAAGA SEQ ID NO1:1688 WBCO41BO5_V1.3_at AATGCTTGAATTGTACACTTCTAAG SEQ ID NO1:1689 WBC041B05_VI.3_at AATATTTGAATCTTATGTGTAACCA SEQ ID 1.1:1690 WBC041B05_Vl.3_at CCAAGATTTGATGGGATTTATCGGT SEQ ID NO1:1691 WBCO41BO5_V1.3 at GCAAGAGCTTGTTTATATTTCATAC SEQ ID NO:1692 WBCO41BO5_V1.3 at GTAGATAGCTCTATAATGCTTGAAT SEQ ID N0:1693 WBCO41BO5_V1.3 at TGGGTTTTAGTTCTTTCTGTGCCCT SEQ ID NO1:1694 WBCO41BQ5_V1.3_at TCATACTTTTTATACTTTGAGGAAA SEQ ID NO1:1695 WBCO41BO5_V1.3_at TTTAGTTCTTTCTGTGCCCTGATAT SEQ ID NO:1696 WBC041B05_Vl.3_at TTCTGTGCCCTGATATTTTGTATAT SEQ ID NO1:1697 WBCO41BO5_V1.3_s-at ATGCCTGCTTAGTGCTTTCTGATTA SEQ ID NO1:1698 WBCO41BO5_1.3_s-at AGCCTCATGAGACTTGGCATACACA SEQ ID 1.1:1699 WBC041B05_Vl.3_s-at ACTCGCATTCTGTTTCTTGCTTTAA SEQ ID NO1:1700 WBCO41BO5_V1.3_s-at TCTTTGCAAGTGCTTTTGGAACTAA SEQ ID 1.1:1701 WBCO41BO5 V1.3_s-at CCCCACAATGATTTTCTTTGCAAGT SEQ ID NO:1702 WBCO41BO5_V1.3_s~at GCTTTCTGATTACTCGCATTCTGTT SEQ ID NO:1703 WBCO41BO5_V1.3_s-at GCAGTTCTGTAGTGTCATTTCTTAT SEQ ID NO:1704 WBCO4I.B05 V1.3 s at GTTTAAAGCCTAACACCATTCTAAT SEQ ID NO1:1705 WBC041B05_V1.3_s at GGGATTCCAGTTATTACGAGTTGCT SEQ ID 1.1:1706 WBCO41BO5 VI.3 s at TCTTGGATTAACTGATGCCTGCTTA SEQ ID 1.1:1707 WBCO41BO5_V1.3_s-at TACACACACACTCATGGGATTCCAG SEQ ID NO:1708 WBC43EO3_V1.3 at ATGACCCGAGAGGTGCAGACCAATG SEQ ID NO:1709 WBC043EO3_V1.3_at ATCCACTCCATGATGTCTTTGTTAG SEQ ID NO:1710 WBC43EO3V.3_at ATGGGATGGATCTTACTCGTGACAA SEQ ID NO: 1711 WBCO43EO3_V1.3 at ATGGTTATTTGCTTCGTCTGTTCTG SEQ ID NO:1712 WB0043E03_V1.3_at AACTGCCTAACTAACTTCCATGGGA SEQ ID NO:1713 WBCO43EO3_V1.3 at AAGGCTTGCCAGTCTATTTATCCAC SEQ ID NO:1714 WBCO43EO3_V1.3 at GATTCGGAAGACCTCTTATGCTCAG SEQ ID NO:1715 WBC043EO3_V1.3_at GTCTGTTCTGTGTTGGTTTTACTAA SEQ ID NO:1716 WBCO43EO3_Vl.3_at TGACGGATACGAGCCACCAGTGCAA SEQ ID 1.1:1717 WBCO43EO3_V1.3_at TTATGCTCAGCACCAAOAGGTGCGT SEQ ID 1.1:1718 WBCO43EO3_V1.3_at TGACGTCAAGACTACCGATGGTTAT SEQ ID NO:1719 Homo sapiens high mobility group nucleosomal binding domain 4, mRNA_______ WBC43G11V.3_at CAGTTTTGCTTGTCATAOGTCTTTA SEQ ID NO1:1720 IWBC43G11V.3_at CAGTGTTGAATCTTCCAATCCATGA SEQ ID NO:1721 WBC043G11 V1.3 at GACCTGTAACACTGTCTCTTTCATA SEQ ID N.1:1722 -381- PROBE SQUENCE.ZL&, 9 equence> ______________________>~' Identif ier WBCO43G11_V1.3_at GATGGTTTCTGTTCTGACTCACTGG SEQ ID NO: 1723 WBCO43G11_V1.3 at GTCAATTTGTCTAACCTGTGGCAGT SEQ ID NO:1724 WBCO43,Gl1 V1.3_at GTGGCAGTACTATACAATCCTGAGT SEQ ID NO: 1725 WBCO43G11_V1.3_at GGTTGTTGCAGCACCATTTTCTGMA SEQ ID NO: 1726 WBCO43G11 V1.3_at TGAAAAGTTCATCCTTTCCTCACTG SEQ ID NO:1727 WBC043G11_V1.3_at TTTGTGTGGGTCTCTT.GATGGTTTC SEQ ID NO:1728 WBCO43G1IV1.3_at TTAGCCATTTGCTTTTCCATACAAT SEQ ID NO:1729 WBCO43G11 Vl.3 at TTCTTCOTTGAGAGTATCTTGGCTA SEQ ID NO: 1730 WBC133.V1.3_at ATGTTATCTACAGACTTTGGGTGAT SEQ ID NO:1731 WBC133.Vl.3_at AGCCCATAGAATGCACAACACCAAG SEQ ID NO: 1732 WBC133.V1.3_at CAGAGGATTTTTAGGGCAGTGAAAC SEQ ID NO:1733 WBC133.V1.3_at CAGCTATTATGATCCTGAATGTATA SEQ ID NO: 1734 WBC133.V1.3_at GCAGGTAACAGAGCACAGAGGATTT SEQ ID NO: 1735 WBC133.V1.3_at GAGAAAACCCTAATGTTATCTACAG SEQ ID NO:1736 WBC133.V1.3_at GTAAACACAGGAAATCTGAACCAGA SEQ ID NO: 1737 WBC133.V1.3_at GTCTGATACTTTAACAGTGGACACA SEQ ID NC:1738 WBC133.V1.3 at GTGGACACATGTCATTATACGTTTG SEQ ID NO:1739 WBC133.V1.3_-at GGCAGTGAAACAATTCTGTCTGATA. $EQ ID NO:1740 WBC133.V1.3_at TATACGTTTGTTTAAGCCCATAGAA SEQ ID NO:1741 Mst3 and SOKI-related kinase (MASK)________ WBC166.gRSP.V1.3_at TTTAGTCAAAGTGCCCATTACCTCC SEQ ID NO: 1742 WBC166.gRSP.V1.3 at AAAATTTTCACCTGCTGTCTAACTG SEQ ID NO:1743 WBC166.gRSP.V1.3_at CATTACCTCCTCTGTTTTTGTAATA SEQ ID NO:1744 WBC166.gRSP.V1.3_at CTGCTGTCTAACTGAAATTCCATTA SEQ ID NO:1745 WBC166.gRSP.V1.3_at GAAATTCTTTTCATTGGTGCCTGTA SEQ ID NO:1746 WBC166.gRSP.Vl.3_at GTTTGGATCTGCACAATTGGGTTTT SEQ ID NO: 1747 WBC166.gRSP.V1.3_at GTTAGTAGTCCTGTAAAGTGTTTCT SEQ ID NO: 1748 WBC166.gRSP.V1.3_at GGTGCCTGTACTGTAACAATTACTT SEQ ID NO;1749 WBC166 .gRSP . Vi.3_at GGGTTTTTGCACAGAAGTCATTTTT SEQ ID NO: 1750 WBC166.gBSP.V1.3 at TCTAGGTGAAGCATACTCCAGTGTT SEQ ID NO:1751 WBC166.gRSP.Vl.3_at TTGACGACACAACTGTATCATGGAT SEQ ID NO: 1752 CGG triplet repeat binding protein 1 (CGGBP1), WBC434.gRSP.V1.3 at ATGGAGGCTCCATACCTAAGTCAGA SEQ ID NO:1753 WBC434 .gRSP .Vi.3 3_at AACTGCATCGCTTCAGTGCAACAGT SEQ ID NO: 1754 WBC434.gRSP.V1.3_at AAGACTGCTTTGTATGTGACTCCCC SEQ ID*NO: 1755 WBC434.gRSP.Vi. 3_at AAGGAGGCTACCACCATTGTGATCA SEQ ID NO: 1756 WBC434 .gRSP .V1.3_at AAGTCTGCCATTAGTGACCACCTCA SEQ ID NO: 1757 WBC434 .gRSP .Vi.3_at CTGAATCATGTTCGCAAGTCTGCCA SEQ ID NO: 1758 WBC434.gRSP.V1.3_at CAGCTCCTCAACTCACAAGATTGTT SEQ ID NO:1759 WBC434.gRSP.Vi.3 -at GCACTTCTTGCAATGTGGTTCTGAA SEQ ID NO:1760 WBC434.gRSP.V1.3_at GGAGGAAAACTCTTCTGCACTTCTT SEQ ID NO:1761 WBC434 .gRSP .Vi. 3_at GGAGGCCAACATCCCACTTGAGAAG SEQ ID NO: 1762 WBC434.gRSP.V1.3_at TTCCTGTCTCGCCACGTGAAGAATG SEQ ID NO:1763 -382 - Probe* Set *? .!. PROBE.. SEUNE fj ~~ euenc * . .).k~~~ .. .. , IdentiE.e; Homo sapiens nmPNAi; CDNA DKFZp667NO84 _______________ WBC493.V1l.3_at AGTGTCACAGTACATtTTCAAGTTT SEQ ID NO:1764 WBC493.V1.3_at ACAGTGCCTCTGTATGCTTTTTGTA SEQ ID NO:1765 WBC493.V1.3 at AACGCTTCTTTATTTTTGATACACA SEQ ID NO:1766 WBC493.V1.3_at CAGACTGCAGTCGTACTTGATTTTT SEQ ID NO:1767 WBC493.V1.3_at CCAGTTCATCTTTAGCTTTCGTTGT SEQ ID NO:1768 WBC493.V1.3_at GAACTGCACAGTCCTAATAATCAAA SEQ ID NO:1769 WBC493.V1.3 at GATACCTCTTAAACTTATGTCTTTT SEQ ID NO:1770 WBC493.V1. 3 at GATATATCCCTTTAGCATTACCTTA SEQ ID NO:1771 WBC493.Vl.3 at GTTTAGACTTGAATCCCAGTTCATC SEQ ID NO:1772 WBC493.V1.3_at TGTTTCCTATTTTTTGATACCTCTT SEQ ID NO:1773 WBC493.V1.3 at TCGTTGTGCTTTTTTAACGCTTCTT SEQ ID NO:1774 Zinc Finger Protein 198________ _ WBC59O.V1.3_at ATGTTTTCGCTTTTATTGTTATGTG SEQ ID NO:1775 WBC59O.V1.3 at AGAGTGTATGCCTATTTTTATGTTG SEQ ID NO:1776 WBC590.V1.3_at ACTTGTGATTTCTTTCTTTTGAGGA SEQ ID NO1:1777 WBC590.V1.3_at AAGCAGCATCTTTGTTACGTTAAAT SEQ ID NQ:1778 WBC590.V1.3_at AAGTTTGGTTGATTTTCTGTTCTGA SEQ ID NO:1779 WBC59O.V1.3 at GAACAAGCGTTATCATCATTATTAT SEQ ID NO:1780 WBC59O .V1 .3 at GATGTGAAACTGCACCTTTTTGCTA SEQ ID NO: 1781 WBC590.V1.3_at GGCTTAAATTTATCCATACCAGTTT SEQ ID NO:17B2 WBC590.V1.3_at GGTATTTGAGGACTGACATTTGACA SEQ ID NO:1783 WBC590.V1.3_at GGCACTTGTTAATTTTTTCAGTCTG SEQ ID NO:1784 WBC590.Vl.3_at TTCAGTCTGTCAATTCACACCTTTT SEQ ID NO:1785 No Homology BM780906.V1.3_at AGCTGAAACACATCTCTTGGGTCCT SEQ ID NO:1786 BM780906 .Vi. 3_at GCTTCCCATCATAGTTTTGCCGTTA SEQ ID NO: 1787 BM780906.Vi.3_at GATTCCCAGAATGCCATCGATGACC SEQ ID 140:1788 BM780906 .Vi.3_at GTTCCGTTTTCAAGGACCAGTCAGC SEQ ID NO: 1789 BM780906.Vl.3 at GTAACAGTGACTCCTGATTCCCAGA SEQ ID NO:1790 BM780906.Vi.3_at GTGTGAGCAGCTCCTCCTGTATAGT SEQ ID 140:1791 BM780906.Vl.3_at TGGAGCTTTTGCCTGTAGCTTGAGA SEQ ID NO:1792 BM780906.V1.3_at TGTATAGTCCTCTTCTTCACTGAAT SEQ ID 140:1793 BM780906.Vi.3_at TCAGTACGTCAGTGGTGGAGCTTTT SEQ ID NO:1794 BM780906.V1.3_at TTCACTGAATGCTGGAACCTCCAAC SEQ ID 140:1795 BM780906.V1.3_at TTTACCCGCAGTATCAAGCACAAGA SEQ ID 140:1796 B1961054.V1.3 at TCAGTAGTAACTCTGCCTTGGCACT SEQ ID 140:1797 B1961054.Vl.3_at ATATGTCAAGCCCTAATTGTCCCCG SEQ ID NO:1798 B1961054.V1.3_at ATGGTTCATCATCCTGAGCTGTTCA SEQ ID 140:1799 B1961054.Vi.3_at AATTAGCTGCTACTACTCCTGCAGG SEQ ID 14:1800 B1961054.V1.3_at CAACGTGTTGAGATCATTGCCACAA SEQ ID NO:1801 B1961054.V1.3_at GCCATCATTTCCCTGCATACAGTAT SEQ ID NO:1802 B1961054.V1.3_at GAATCCAGAGTCCAAGACCGTCAAG SEQ ID NO: 1803 B1961054.V1.3_at GGTACTACTGATACGGATGGCCCAA SEQ ID NO:1804 -383- * pobe'S~ ~1znPR~OBE- SEQUNCE< Sac ____ ___ ___ ___ ____ __ ___ ___ ___ ____ ___ ___ ___ ___ Identifie~r B1961054.V1.3 at GTTCTCCTAAGATGACCAACCAGTC SEQ ID NO:1805 B1961054.Vl.3_at GGTCTAAAAGATCTCCTCGAACACT SEQ ID NO: 1806 B1961054.V1.3 at TAATTGTCCCCGGATTGCAGTTCTC SEQ ID NO:1807 -384- TABLE 3 AMINO ACID SUB-CLASSIFICATION Sub-classes Anino acids Acidic Aspartic acid, Glutamic acid Basic Noncyclic: Arginine, Lysine; Cyclic: Histidine Charged Aspartic acid, Glutamic acid, Arginine, Lysine, Histidine Small Glycine, Serine, Alanine, Threonine, Proline Polar/neutral Asparagine, Histidine, Glutamine, Cysteine, Serine, Threonine Polar/large Asparagine, Glutamine Hydrophobic Tyrosine, Valine, Isoleucine, Leucine, Methionine, Phenylalanine, Tryptophan Aromatic Tryptophan, Tyrosine, Phenylalanine Residues that influence Glycine and Proline chain orientation -385- TABLE 4 EXEMPLARY AND PREFERRED AMINO ACID SUBsTITUTIONS Original Residue Exemplary Substitutions Preferred )__Substitutions Ala Val, Leu, Ile Val Arg Lys, Gin, Asn Lys Asn GIn, His, Lys, Arg Gin Asp Glu Glu Cys Ser Ser Gin Asn, His, Lys, Asn Glu Asp, Lys Asp Gly Pro Pro His Asn, Gin, Lys, Arg Arg Ile Leu, Val, Met, Ala, Phe, Norleu Leu Leu Norleu, Ile, Val, Met, Ala, Phe Ile Lys Arg, Gin, Asn Arg Met Leu, Ile, Phe Leu Phe Leu, Val, Ile, Ala Leu Pro Gly Gly Ser Thr Thr Thr Ser Ser Trp Tyr Tyr Tyr Trp, Phe, Thr, Ser Phe Val Ile, Leu, Met, Phe, Ala, Norleu Leu -386- N 0n 0 C 00, t.O 'o 0 0 0 0 % N 0n 0 rn C4 40 0 e 9ih0 on 00 0 V v 00 r- - 0 i ,C i -i - q W %n 00o 040 W (Z 00 9 - sNclr - 0 "t't 0 N~~ o C C, C 0 O\ C> N C04 N asN N "o N N - N N t- a - No w N w q -, In v -- m-oN N t n -i i 9 gN0N N0t "t' 1 N 9 N'* N 000C 90 0 0 qT rr- N t% w " w 0 kn 0 000~0 9 ' N Ns N N a% o N o o No N N N N N N N Ni N as u- enV 0o 0 D Go co N- N - '0 '0 0 '0 00 00 0 ~~ en'~ O 9 0 ~0 tDMu ,% Ch G\ r-N mO ' 000 00'0 0'00 N 0 00 000 m0 Qm1 Cu1 Cu 14 q%0 0 N0%Q ~Cu- - ; 0 14 C 9n 00 00 )0 n v 0o 9 0D r 0 m~ NO d m N% Q -s 0%> ~a. to 0 c.0 It, 00 at m 0 CD * CO 0 0o m -r - o% h o% cs %o d - - mo % %o % C% C? 9 m% 0% 9 9 % .ON t- CY at, ON ar 0000 0 .0 tn~~ CD -00 0 F 90%9 9 9 9 ' 9 9 9 9t 9 009 9 9 09 9 0 w 0 0 0 0 0 0 0 - 0000 ;0 w w wa w 0 w% Cu m 0 W-uwm -i O~ V W M ON99 M N 0k0at 00 oo %~ C e ~ ~ t 00 ca (D - - in en v w~0 m'% o- r o 0 N 10 0 C> N Gu - -U can N Nn N N .0 '0 '0 '0'0 0 ' . . 0 . . .

000 CC! cat 9 00C)C CuN CD 0 Q D n 00 en atCt 0CD 0C 0 'n .~ 00 0 Ge 0n 0De n0m 0wC n% CD 40C D q( 0 0 0 0 0 '.0 0 QA ; o% 0 =C 01 tr - 0 00 0 00, t-v v t-v t00 -v N Nnm% -O t- ON w ntn "k ... C >0 00 00 9w9 w w voto ON 0 NQ N %n Cu q c - o-, -~ 'q'0 It 000 CCD .0 mO 0(D%'0 N ' %oin t o O %n 0n in 0000 0n .~ .- O . 0n '0 tn tn %nn.o% - - - -m -: c- S 00 m m A nt C0 0 en n C4 - n0 Z ~ 0 0 0 '000 %D m O 0 N0 %. w w n n0 N N N e 0, en 0 C N o N N0% N NN % CS Q * .It A 'D 'D RAA " " A t t A' A ' 1 ' t t *.co 00 0 m0 QQ O O O 9 9 9 9 ClCD Cp 0< Q C14 00 on, -. 000e 00 0 0 1 0-0 n en6 n0 CD C- 0 .0j CD N5C ' D Q 0k 0 C> 0 0 o o 0 C o Q Q q 9C7 a W9 N W - 0 t 0 0~ 00 k 0 nNc 0 00 > InC 04Q 00 -n ) 00 ' - 00 V: NC Nq 0 N ~ IA 0 N AI '0 en-R' ql '.0qq-w;. q 'R I . q 0C0C 0 - Ch 0 0 Ch N ' r N N Q% -N t ON- v 0% '.h 0D 0 W~0 I 00 00 0 9wWW D 0 0C 00 w A w 00 ',c,0 'c ,' . Cl, 0 IA 0Cl Ql Cl 0 Q 0A c) Q 0 f*0 0 ' 4 0 00 N 0 0 0 Q~ R - -~ 00 rn ~ Q O Oo O Oen eno 00 D u up m 400 Cun 030 CuC 9n 0 00 ON 00. 0i ' 0%0 0C 9* 9% 00 0 0 C 0004 -n 0% U t CuCD 40 00 - 0m% 00 ON 0 0 cn vo 6 nC w 9 Q- ON 10 - Q Q-> c 9 CA .'.4 C1 m C40 C) flc' 99 -'.-0 c- . C- q- q q 4N w-~ ~ ' a\ %-0 0'm * 6r .00 00 6D doo% o - ~ ~ ~ ~ ~ ~ 4 0~ 0 - 0 0% Q-~ ~ C- ~ ~ 0 0 o( ~ 0 Q00 Q -00% ( N '0 0 40 -oN- CD0 0 0 0 Cp6 t- -N0% N t-0 N -0 - ONt 0C N N 0 1 Cu ( w tt - - -R U Ic S0 0 t- V - 0,t '0 0' CD 14*'0 '0 - % 0 '. . . Q 0 p 0 M %n 0> 0 0 00 0 00 uu 0 0 0 0 0 0 0 TABLE 6 GENE PRIORITY ORDER BASED ON T VALUE Gene Name Day M t P.Value B WBC008F06_V1.3_at 9 -0.53075 -7.92738 8.8E-10 21.27623 WBC007G12_V1.3_at Q -0.34772 -6.96751 2.09E-07 16.05095 WBCOOIF11_V1.3_at 9 -0.53926 -6.96303 2.15E-07 16.03718 WBC014GO8_V1.3_at 9 -0.50112 -6.67446 1.04E-06 14.53887 WBC013EIO_V1.3_at 2 -0.44979 -6.64137 1.24E-06 14.37086 WBC012EO7_V1.3_at 0 -0.46294 -6.47256 3.05E-06 13.50699 WBC024C12_V1.3_at 0 -0.44376 -6.12738 1.85E-05 11.79847 WBC006HO6_VI.3_at 7 -0.42431 -6.11448 1.97E-05 11.73829 WBC030D02_V1.3_at 7 -0.47564 -6.08505 2.28E-05 11.59508 WBC006EO3_VI.3_at 9 -0.48246 -6.03644 2.92E-05 11.35935 WBC028F05_VI.3_at 0 -0.48118 -6.02243 3.15E-05 11.29056 WBC009E12_VI.3_at 9 -0.7531 -6.01545 3.25E-05 11.25809 WBC018DO5_V1.3_at 7 -0.51854 -6.00257 3.47E-05 11.19618 WBC01OF04_V1.3_at 4 -0.76635 -5.9324 5.04E-05 10.76647 WBC013A09_V1.3_at 9 -0.32137 -5.92857 5.04E-05 10.84143 WBC001F08_V1.3_at 7 -0.31702 -5.91162 5.49E-05 10.76031 WBC166.gRSP.VI.3_at 9 -0.70207 -5.87988 6.43E-05 10.60961 WBC024BO5_V1.3_at 7 -0.4822 -5.82594 8.41E-05 10.35363 WBC004DO7_V1.3_at 9 -0.38487 -5.81519 8.87E-05 10.30359 WBC032BO5_V1.3_at 7 -0.42227 -5.80372 9.38E-05 10.24879 WBC021DOI_VI.3_at 7 -0.37385 -5.75613 0.000118 10.02519 WBC041B05_VI.3_at 9 -0.60661 -5.69821 0.000158 9.755808 WBC493.VI.3_at 7 -0.75113 -5.63393 0.000215 9.456588 WBC001C11_V1.3_s_at 9 -0.459 -5.60169 0.000252 9.309492 WBC019B05_VI.3_at 0 -0.57447 -5.60118 0.000256 9.309371 Foe545.VI.3_at 9 -0.40775 -5.58788 0.00027 9.246056 WBC043G11_VI.3_at 7 -0.3362 -5.58774 0.000268 9.243826 WBC004C03_V1.3_at 0 -0.41087 -5.56794 0.0003 9.157128 WBCOO1A07_V1.3_at 9 -0.53398 -5.55969 0.000309 9.116868 BM734719.VI.3_at 2 -0.41143 -5.55799 0.000313 9.108264 WBCO18BO1_V1.3_at 7 -0.67086 -5.53604 0.000344 9.00706 Foel072.V1.3_at 7 -0.49276 -5.5316 0.000351 8.986814 WBC007GO3_V1.3_at 9 -0.77183 -5.51378 0.000385 8.90749 WBC004E04_V1.3_at 7 -0.3488 -5.4981 0.000412 8.834262 FoelO60.V1.3_at 9 -0.4171 -5.43881 0.000551 8.568091 WBC590.V1.3_at 9 -0.46943 -5.42207 0.000596 8.492765 -392- Gene Name Day M t . P.Value B WBC0OH09_V1.3_at 7 -0.55531 -5.41491 0.00061 8.458322 WBC027DO7_V1.3_at 0 -0.39411 -5.40118 0.000667 8.402682 WBC013CO3_V1.3_at 9 -0.29677 -5.36572 0.000778 8.240336 WBC024C11_V1.3_at 2 -0.29424 -5.36158 0.000799 8.220603 WBC016A12_V1.3_at 0 -0.48188 -5.36119 0.000806 8.224168 WBC012GO2_V1.3_at 7 -0.53236 -5.34123 0.000863 8.128662 BM781417.V1.3_at 0 -0.54661 -5.32386 0.000961 8.05831 BM781186.V1.3_at 0 0.607083 5.346723 0.000863 8.159792 BM735441.V1.3_at 0 0.253862 5.44514 0.000541 8.600034 B1960933.V1.3_at 7 0.716823 5.454949 0.000506 8.638769 BM735167.V1.3_at 2 0.414248 5.46725 0.000484 8.695428 BM735545.VI.3_at 0 0.589494 5.471981 0.000476 8.721067 B1961494.V1.3_at 7 0.354654 5.513986 0.000382 8.906528 BM735409.VI.3_at 0 0.269757 5.568459 0.0003 9.159479 BM735519.V1.3.at 0 0.323515 5.588238 0.000272 9.250006 019717252-3M_at 2 0.63348 5.591229 0.000267 9.260645 BM735286.VI.3_at 0 0.247435 5.648946 0.000203 9.529213 WBC039F12_V1.3_at 0 0.351171 5.66273 0.00019 9.592888 BM735102.VI.3_at 0 0.356539 5.707416 0.000152 9.800038 WBC027EO7_V1.3_at 0 0.290616 5.708292 0.000152 9.804113 WBC008F12_VI.3_at 0 0.269626 5.75662 0.000119 10.02939 BM734457.V1.3_at 7 0.430304 5.905849 5.65E-05 10.73278 B1961109.V1.3_at 0 0.72204 5.929105 5.05E-05 10.84356 BM734531.V1.3_at 0 0.633646 5.932699 4.96E-05 10.86069 WBC028DO9_VI.3_at 0 0.291809 5.937444 4.84E-05 10.88332 BM735166.V1.3_at 0 0.357974 5.981577 3.88E-05 11.09433 WBC026EO2_VI.3_at 0 0.339222 6.005673 3.43E-05 11.20996 WBC003HOI_V1.3_at 0 0.398243 6.012941 3.31E-05 11.24489 WBC022BO6_VI.3_at 2 0.431945 6.027528 3.06E-05 11.31647 WBC013HO3_V1.3_at 0 0.472666 6.093231 2.2E-05 11.6326 BM735450.V1.3_at 0 0.292831 6.119368 1.92E-05 11.75951 B1961637.V1.3_at 2 0.525483 6.147262 1.66E-05 11.89799 B1961711.VI.3_at 0 0.364045 6.152405 1.62E-05 11.92041 WBC038GI1_V1.3_at 0 0.409732 6.174059 1.45E-05 12.02617 BM735534.V1.3_at 0 0.372736 6.209232 1.21E-05 12.19843 WBC028EO7_V1.3_at 2 0.582508 6.220488 1.14E-05 12.25714 WBC020B04_VI.3_at 0 0.418213 6.266942 8.98E-06 12.48239 WBC005FIO_VI.3_at 0 0.472342 6.27517 8.6E-06 12.523 BM735457.V1.3_at 2 0.410421 6.319517 6.8E-06 12.74701 -393- Gene Name Day M t P.Value B WBC007AO9_VI.3_at 0 0.568251 6.341687 6.08E-06 12.85253 BM735352.V1.3_at 2 0.628248 6.403566 4.38E-06 13.16644 BM735576.VI.3_at 0 0.472577 6.445128 3.53E-06 13.36913 WBC014HO6_VI.3_at 2 0.785821 6.455537 3.33E-06 13.42745 WBC003FO2_V1.3_at 7 0.367974 6.516236 2.42E-06 13.73495 BM735536.V1.3_at 0 1.024189 6.55447 1.97E-06 13.92057 BM734654.V1.3_at 0 0.802667 6.597475 1.57E-06 14.13893 WBC009B1O_V1.3_at 2 0.664414 6.599032 1.55E-06 14.15456 WBC028CO1_V1.3_at 0 0.290434 6.655002 1.15E-06 14.43232 BM734865.VI.3_at 0 0.656049 6.698282 9.12E-07 14.65401 WBC012FO7_V1.3_at. 0 0.584337 6.702508 8.91E-07 14.6757 BM780906.V1.3_at 0 0.416052 . 6.772214 6.11E-07 15.03457 WBC022BO5_V1.3_at 2 0.646312 6.799413 5.27E-07 15.18522 WBC003D11_VI.3_at 2 1.337346 6.914252 2.81E-07 15.78363 WBC024FO8_VI.3_at 2 0.518276 6.997403 1.78E-07 16.22033 B1961671.V1.3_at 0 0.453662 7.077614 1.14E-07 16.63083 WBC434.gRSP.V1.3_at 2 0.448914 7.087078 1.08E-07 16.69443 BM781174.V1.3_at 0 0.618002 7.120547 8.96E-08 16.85824 B1961885.VI.3_at 0 0.983887 7.169149 6.83E-08 17.11655 BM781334.V1.3_at 0 0.475758 7.183024 6.32E-08 17.19046 WBC030C04_V1.3_at 0 0.602389 7.22709 4.93E-08 17.42568 B1961443.VI.3_at 0 0.505935 7.272533 3.82E-08 17.66902 G11592834.VI.3_at 0 0.611795 7.345617 2.53E-08 18.06199 gi576646.V1.3_s_at 0 1.280838 7.399041 1.87E-08 18.35048 BM781178_unkn.V1.3_at 0 0.386001 7.452231 1.38E-08 18.63874 WBC032GO5_V1.3_at 0 0.596733 7.452338 1.38E-08 18.63932 WBC021BOS_VI.3_at 2 0.792947 7.524122 9.14E-09 19.04904 B1961682.VI.3_at 0 0.545432 7.553677 7.71E-09 19.19129 BM735573.VI.3_s_at 0 0.483434 7.568776 7.07E-09 19.27384 WBC022FO8_VI.3_at 0 0.553469 7.608824 5.61E-09 19.49316 BM735585.V1.3_at 0 0.402875 7.613483 5.47E-09 19.51871 B1961620.VI.3_at 0 0.584057 7.704254 3.23E-09 20.01797 BM734722.V1.3_at 0 0.736865 8.435653 4.27E-11 24.13395 BM735487.VI.3_at 0 0.445341 8.825278 4E-12 26.38603 WBCOO1CI2_V1.3_at 9 0.76454 8.834995 3.77E-12 26.47277 B1961941.V.3_at 0 0.478102 9.36128 1.45E-13 29.53961 BM734862.V1.3_at 0 0.727226 9.401378 1.13E-13 29.77781 WBC005DO2_VI.3_at 0 0.680964 11.60693 8.19E-020 43.19762 BM734889.V1.3_at 0 1.083673 11.66465 5.62E-020 43.55399 -394 - The priority ranking of genes is based on increasing value of t value for the first day each gene is significant (p<0.001) following stress induction, and for genes that were significant for at least three sampling times. -395- TABLE 7 Two GENES SELECTED Genes Sensitivity Specificity Success WBC001F1I B1961443 0.926829268 0.802816901 0.881443299 WBC030D02 BM735536 0.918699187 0.802816901 0.87628866 WBC030D02 BM735536 0.918699187 0.802816901 0.87628866 B1961443 WBC027DO7 0.910569106 0.816901408 0.87628866 B1961443 WBC030D02 0.910569106 0.816901408 0.87628866 BM735536 BM734865 0.886178862 0.816901408 0.860824742 BM735536 B1961494 0.894308943 0.802816901 0.860824742 BM735409 B1961443 0.926829268 0.746478873 0.860824742 WBC01OF04 WBC003HO1 0.918699187 0.76056338 0.860824742 BM734865 BM735536. 0.886178862 0.816901408 0.860824742 WBCOOC11 B1961443 0.918699187 0.746478873 0.855670103 BM735576 BM735536 0.902439024 0.774647887 0.855670103 B1961443 WBC030C04 0.886178862 0.802816901 0.855670103 WBC004D07 B1 961443 0.894308943 0.774647887 0.850515464 B1961443 WBC003D11 0.869918699 0.816901408 0.850515464 B1961443 WBC004DO7 0.894308943 0.774647887 0.850515464 WBC012G02 WBC028DO9 0.894308943 0.774647887 0.850515464 BM735536 WBC019BO5 0.886178862 0.788732394 0.850515464 B1961443 BM734719 0.886178862 0.788732394 0.850515464 B1961443 WBC021B08 0.886178862 0.788732394 0.850515464 -396- TABLE8 THREE GENES SELECTED Genes Sensitivity Specificity Success B1961443 WBC004E04 B1961620 0.910569106 0.873239437 0.896907216 B1961443 BM735441 BM735536 0.943089431 0.802816901 0.891752577 WBC003HO1 WBC004E04 BM735536 0.93495935 0.802816901 0.886597938 B1961443 B1961494 Foe545 0.910569106 0.845070423 0.886597938 WBC028DO9 B1961443 BM735487 0.918699187 0.830985915 0.886597938 Foe545 WBC013EI0 B1961443 0.93495935 0.802816901 0.886597938 WBC027EO7 WBC01O0F04 B1961443 0.910569106 0.830985915 0.881443299 B1961109 WBC013C03 BM735536 0.910569106 0.816901408 0.87628866 BM735487 WBC028DO9 WBC021DO1 0.894308943 0.845070423 0.87628866 WBC041B05 WBC028D09 WBC019B05 0.910569106 0.816901408 0.87628866 WBC030DO2 BM735536 WBC01 8D05 0.902439024 0.816901408 0.871134021 B1961443 WBC030DO2 WBC012FO7 0.910569106 0.802816901 0.871134021 WBC003D11 B1961620 B1961443 0.894308943 0.830985915 0.871134021 Foe545 WBC007GO3 B1961443 0.918699187 0.788732394 0.871134021 WBC003DII B1961443 WBC590 0.894308943 0.830985915 0.871134021 WBC003D11 WBCOOC12 B1961443 0.894308943 0.816901408 0.865979381 B1961443 BM735585 WBCOOIFl1 0.894308943 0.816901408 0.865979381 WBC009EI2 BM735536 BM735167 0.894308943 0.816901408 0.865979381 WBC028EO7 BM735536 WBC493 0.902439024 0.802816901 0.865979381 B1961682 B1961443 WBC493 0.910569106 0.788732394 0.865979381 -397- TABLE 9 FouR GENEs SELECTED Genes Sensitiity Specificity Success B1961443 WBC019BO5 WBCO24C12 BM735585 0.93495935 0.85915493 0.907216495 WBC006EO3 WBC030CO4 WBC003D1 1 B1961443 0.926829268 0.85915493 0.902061856 WBC021D01 BM735536 B1961443 WBC020B04 0.93495935 0.845070423 0.902061856 B1961443 BM734862 BM735536 WBC007GO3 0.93495935 0.845070423 0.902061856 BM735536 B1961671 WBC038GI1 WBC003H01 0.93495935 0.830985915 0.896907216 WBC027D07 B1961711 B1961443 BM735487 0.926829268 0.830985915 0.89175257 BM734722 B1961443 WBC028EO7 WBC030DO2 0.886178862 0.901408451 0.891752577 B1961885 B1961443 B1 961620 WBC041 B05 0.910569106 0.85915493 0.891752577 BM735536 B1961109 Foe545 WBC001Fl1 0.910569106 0.845070423 0.886597938 B1960933 B1961885 B1961443 WBC012GO2 0.902439024 0.85915493 0.886597938 WBC007AO9 WBC166 WBC028D09 WBC005F1O 0.910569106 0.845070423 0.886597938 B1961443 BM735457 WBC030CO4 WBC008FO6 0.886178862 0.873239437 0.88144329 WBC024FO8 BM735536 WBC022BO5 B1961109 0.902439024 0.845070423 0.881443299 WBC019BO5 BM735167 WBC008F12 BM735102 0.894308943 0.85915493 0.881443299 WBC028F05 WBC003HO1 B1961443 BM735536 0.918699187 0.816901408 0.881443299 WBC005DO2 BM781174 WBC028D09 WBC166 0.910569106 0.830985915 0.881443299 G11592834 BM735534 B1961443 WBC004EO4 0.902439024 0.845070423 0.881443299 WBC001F08 BM734457 B1961443 WBC039FI2 0.902439024 0.830985915 0.87628866 WBC01OF04 WBC007GO3 BM735102 B1961443 0.918699187 0.802816901 0.87628866 BM735536 WBC038G11 BM781334 BM734865 0.894308943 0.845070423 0.87628866 -398- '0 n001 (00000000 -- o O~ I-M M 0 CO~ ~ 0 (0 0 WN N 0 M1 0000 '--' 0-' 0 l0 m r- Nc, rl -N-rm - N 21 '- - 0 D (0)O 0 0010101) 0)0)0) 0)OD 0 0 C 0) C) 0) 0C)0000) 0) )0) 00O -0 0O 00 00 00 1 D00 to V C) 10 (V t) 0V U) 1r)CV' 0V Wv ID Cv) 0 0 U) N - - VII T- CV) co - Fl-'V-'- N-ON 'T- 00 -0 0 T cr () ) ) Y)N a) 0D 0 0) 0) 0 It* 0 M) 0) 0 0Y) 0) 0) r- 10 1) 1O 10 CV) 0 10) 10) 1 In W0 v- 10 10 0 10) (0 0 10 0(0 10100 DO NO - CID1 V( O 00-C V Q - V 0 0( ( NDt) t - (Y O (0 CVCV c ) (0((OR CV) C0;(( 6 J (0 ( 0( ( N R6 O qq C C0)00C 0) 0 (0 00 0 0 0 0 N 0) to 0) N - w 0) N - f- N 0 '- -w N1- - 01 (0 N- m V m0 ) l ow 0mmw0m00 0 0 (D 0 ) Q w v w0 0 .- 0 0( C 0(0Cq )~ 10qq q ON3N 0 0 0 ( 0 aa 0 0 0 0 10 o0 0 , v c) V0 m LL oh% w mm mwLL i o)0 ~ 0 q tN- D 040 0 r o01 10q N 0) a) co(" mN -0 A 0 00010 (0 00 qT 00 t 00m mc 3 o )M oca c 0'- U') U) 0 0 0 N) (0)'- 0 -V m Go T- 0 *4 )'- - 0M1 CD) N 0- lo- V 10 mt '-) N- 04 T- V LC) N C> CVO1 N (0 )0 0 0 0 ce) m 0 0N'm CC) C w 0co c '- CF G) m c ) 0 T coO~ CE-399oooddd ooooowooddd NC')0)C 0)0 2 ~ DN C - N N C -CR Nq c- cD CD CR .- CR '- 0R N 0 ) 0 0 0 Nc 0) N 0 0 0 0 0 0 0 0 0 666 odd do VO8aO L*' M Oo) 0 V0 0) 0o 0) 0M CD CD CD a20 ) 0) 0) 0) 0) 0) 0) D ) a0 C N 10 ClD oo 020) 0V r- N r- 0 OD r- P- W- W- M2 W-0 0 0 0 0 0 0 0 0 0 0 0 0 0 ~~10 (00 0 QCDC00 Ow Ow 0 Go CD 00- 02w CDNN0 0 0 02o 120 0200 0 0U CDCDN c)U' 0 CDC C0 P- N) 00Q0 0 0D00 ~ N 0)o to to TO V - 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Claims (18)

1. A method for determining the presence or absence of allostatic load in a test subject, wherein the allostatic load results from athletic training, the method comprising comparing expression of at least one stress marker gene in a leukocyte sample of the test subject to expression of at least one corresponding stress marker gene in a control leukocyte sample of a normal subject or a subject lacking allostatic load resulting from athletic training, wherein a difference in the expression between the sample and the control indicates presence of allostatic load resulting from athletic training, wherein a similarity in the expression between the biological sample and the control indicates absence of allostatic load resulting from athletic training, wherein the at least one stress marker gene is selected from the group consisting of: (a) a gene having a polynucleotide expression product comprising a nucleotide sequence that shares at least 80% sequence identity with the sequence set forth in any one of SEQ ID NO: 23, 24, 33, 56, 62, 87, 103, 135, 145, 148, 151, 156, 158, 160, 163, 165, 171, 182, 184, 186, 190, 198, 202, or 208, or a complement thereof; (b) a gene having a polynucleotide expression product comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 88, 104, 136, 146, 149, 152, 157, 159, 166, 172, 183, 191, 199, 203, or 209, (c) a gene having a polynucleotide expression product comprising a nucleotide sequence that encodes a polypeptide that shares at least 90% sequence similarity with the sequence set forth in SEQ ID NO: 88, 104, 136, 146, 149, 152, 157, 159, 166, 172, 183, 191, 199, 203, or 209, and (d) a gene having a polynucleotide expression product comprising a nucleotide sequence that hybridizes to the sequence of (a), (b), (c) or a complement thereof, under high stringency conditions.

2. A method according to claim 1, wherein a difference in expression between the sample and the control is detected for at least two days.

3. A method according to claim 1, wherein a difference in expression between the sample and the control is detected at each of days 0, 1, 3, and 7 after induction of stress.

4. A method according to any one of claims 1 to 3, comprising: (1) measuring in the sample the level or functional activity of an expression product of the at least one stress marker gene and (2) comparing the measured level or functional activity of each expression product to the level or functional activity of a corresponding expression product in the control.

5. A method according to any one of claims 1 to 4, wherein: (i) the presence of allostatic load resulting from athletic training is indicated when the measured level or functional activity of the or each expression product is (a) 10% lower than the measured level or functional activity of the or each corresponding expression product; or (b) 10% higher than the measured level or functional activity of the or each corresponding expression product; or C:NRPortblDCCSZPW7g7186_ LDOC-3/12/2012 - 417 (ii) the absence of allostatic load resulting from athletic training is indicated when the measured level or functional activity of the or each expression product is the same as or similar to the measured level or functional activity of the or each corresponding expression product.

6. A method according to any one of claims 1 to 5, wherein the presence of allostatic load resulting from athletic training is determined by detecting a decrease in the sample relative to the control in the level or functional activity of at least one stress marker polynucleotide selected from (a) a polynucleotide comprising a nucleotide sequence that shares at least 80% sequence identity with the sequence set forth in any one of SEQ ID NO: 24, 33, 56, or 62, or a complement thereof; and (b) a polynucleotide comprising a nucleotide sequence that hybridizes to the sequence of (a) or a complement thereof, under high stringency conditions.

7. A method according to any one of claims I to 5, wherein the presence of allostatic load resulting from athletic training is determined by detecting an increase in the sample relative to the control in the level or functional activity of at least one stress marker polynucleotide selected from (a) a polynucleotide comprising a nucleotide sequence that shares at least 80% sequence identity with the sequence set forth in any one of SEQ ID NO: 23, 87, 103, 135, 145, 148, 151, 156, 158, 160, 163, 165, 171, 182, 184, 186, 190, 198, 202, or 208, or a complement thereof; (b) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in any one of SEQ ID NO: 88, 104, 136, 146, 149, 152, 157, 159, 166, 172, 183, 191, 199, 203, or 209; (c) a polynucleotide comprising a nucleotide sequence that encodes a polypeptide that shares at least 90% sequence similarity with the sequence set forth in SEQ ID NO: 88, 104, 136, 146, 149, 152, 157, 159, 166, 172, 183, 191, 199, 203, or 209; and (d) a polynucleotide comprising a nucleotide sequence that hybridizes to the sequence of (a), (b), (c) or a complement thereof, under high stringency conditions.

8. A method according to claim 5, wherein the measured level or functional activity of an individual expression product varies from the measured level or functional activity of an individual corresponding expression product by no more than about 5%.

9. A method according to any one of claims 1 to 8, comprising measuring the level or functional activity of individual expression products of at least about two stress marker genes.

10. A method according to any one of claims I to 8, comprising measuring the level or functional activity of individual expression products of at least about three stress marker genes.

11. A method according to any one of claims 1 to 8, comprising measuring the level or functional activity of individual expression products of at least about four stress marker genes. C.WRPortbI\DCC\SZP\4886054_1 DOC-5/02/2013 -418

12. A method according to any one of claims I to 11, wherein the sample comprises blood.

13. A method according to any one of claims I to 12, wherein the sample comprises peripheral blood.

14. A method according to any one of claims I to 13, wherein the expression product is a RNA molecule.

15. A method according to any one of claims I to 14, wherein the expression product is a polypeptide.

16. A method according to any one of claims I to 15, wherein the expression product or corresponding expression product is a target RNA or a DNA copy of the target RNA whose level is measured using at least one nucleic acid probe that hybridizes under high stringency conditions to the target RNA or to the DNA copy, wherein the nucleic acid probe comprises at least 15 contiguous nucleotides of a stress marker polynucleotide.

17. A method according to claim 16, wherein the probe for detecting the stress marker polynucleotide comprises a sequence as set forth in any one of SEQ ID NO: 232 333, 261-271, 356-366, 400-410, 433-443, 455-465, 466-476, , 552-553, 598-608,

620-630, 642-652, 653-663, 664-674, 697-707, 719-729, 752-762, 851-861, 1093 1103, 1192-1202, 1346-1356, 1379-1389, 1511-1521, 1566-1576 or 1577-1587. 18. A method according to any one of clainis I to 17, further comprising comparing expression of another stress marker gene in the leukocyte sample to expression of a corresponding stress marker gene in the control leukocyte sample, wherein the another marker gene is selected from the group consisting of (i) a stress marker gene which comprises a nucleotide sequence that shares at least 80% sequence identity with the sequence set forth in SEQ ID NO:178, or (ii) a gene having a polynucleotide expression product comprising a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 179, or (iii) a gene having a polynucleotide expression product comprising a nucleotide sequence that encodes a polypeptide that shares at least 90% sequence similarity with the sequence set forth in SEQ ID NO:179, or (iv) a gene having a polynucleotide expression product comprising a nucleotide sequence that hybridizes to the sequence of (i), (ii), (iii) or a complement thereof, under high stringency conditions. 19. A method according to claim 18, wherein the expression product or corresponding expression product of the another stress marker gene is a target RNA or DNA copy of the target RNA whose level is measured using at least one nucleic acid probe, wherein the probe for detecting the another stress marker polynucleotide comprises a sequence as set forth in any one of SEQ ID NO: 488-498. C:\NRPorbT\CC\SZPI478786_1. OC-3/122012 -419 20. A method according to any one of claims I to 19, wherein the test subject is a horse. 21. A method for treating, preventing or inhibiting the development of allostatic load in a subject, wherein the allostatic load results from athletic training, the method comprising determining the presence or absence of allostatic load in the subject according to the method of any one of claims 1 to 20, and administering to the subject an effective amount of an agent or therapy that treats or ameliorates the symptoms or reverses or inhibits the development of allostatic load in the subject on the basis that the subject tests positive for allostatic load. 22. A method according to any one of claims 1 to 21, substantially as herein before described with reference to the figures and/or examples.