APPARATUS AND METHODS FOR HIGH AVIDITY BINDING OF INTERFERING SPECIES IN SAMPLE ANALYSIS FIELD OF THE DISCLOSURE This invention is directed to compositions, methods and apparatus used for clearing or depleting 5 interfering species in sample analytes. BACKGROUND OF THE DISCLOSURE Laboratory testing plays a critical role in health assessment, health care, and ultimately, the public's health. Test results contribute to diagnosis and prognosis of disease, monitoring of treatment and health status, and population screening for disease. Laboratory testing affects 0 persons in every life stage, and almost everyone will experience having one or more laboratory tests conducted during their lifetime. An estimated 7 to 10 billion laboratory tests are performed each year in the United States alone, and laboratory test results influence approximately 70% of medical decisions (http://www.cdc.gov/mmwr/preview/mmwrhtml/rr5413al.htm). 5 As reported by Markets and Markets (http://www.marketsandmarkets.com/Market Reports/immunoassay-market-436.html) the global immunoassay instruments and reagents market was valued at about $13.0 billion in 2013 and is expected to grow at a healthy CAGR of 8.1% to reach $19.1 billion by 2018. The expanding use of immunoassays, new and innovative product launches by key industry players, increasing demand for high quality healthcare services, .0 and rapidly increasing geriatric population are the major factors driving the global market. The enzyme immunoassays segment accounted for the largest share of 35.2% of the global market in 2012, while the chemiluminescence immunoassays market is estimated to witness tremendous growth in the next five years, as this market comprises of automated systems that offer the highest sensitivity. 25 Infectious diseases, endocrinology, oncology, and bone and mineral segments of the market are projected to witness high growth rates. The usage of lateral flow immunoassay-based point-of care (POC) tests has been on the rise to diagnose various diseases such as oncology, cardiology, and diabetes, and conditions such as pregnancy. In addition, biomarkers are also facing emerging 30 trends in the market that uncovers new growth opportunities for immunoassay companies 1 Interference is defined as "the effect of a substance present in the sample that alters the correct value of the result, usually expressed as concentration or activity, for an analyte" (Kroll & Elin, 1994). Substances that alter the measurable concentration of the analyte in the sample or alter antibody binding can potentially result in assay interference (Tate & Ward, 2004). Interference can 5 have important clinical consequences and may lead to unnecessary clinical investigation as well as inappropriate treatment with potentially unfavourable outcome for the patient (Ismail & Barth, 2001). It is important to recognize interference in immunoassays and put procedures in place to identify them wherever possible (Kricka, 2000) as interference in immunoassays is a serious but underestimated problem. 0 There is a need for a simple, cheap, and effective solution to pre-treat analytic samples, including human serum and plasma specimens in the laboratory to sequester/deplete and mitigate known mechanisms of sample specific interferences, such as human anti-animal antibodies (HAAA) and Manufacturer assay-specific interference (MASI) known to impact the quality of patient results 5 and subsequent patient management SUMMARY OF THE DISCLOSURE Therefore, provided herein are methods and apparatus useful in removing or decreasing interference in an analyte, which do not change the composition or definition of the analyte and .0 which can be used both at the point of care (POC) as well as being amenable to use in large commercial laboratory analysis. Accordingly, disclosed herein are a method to remove or decrease interference in an analyte comprising treating the analyte with a conditioning agent wherein the conditioning agent removes or decreases one or more specific interfering substances in the analyte and wherein the 25 conditioning agent is removed from the analyte prior to analysis and does not add to, change or adulterate the analyte. In some exemplary embodiments, the analyte is a bodily fluid or biological sample. Examples of such analytes include blood, serum, plasma, urine, semen, saliva, stool or mucous. In these exemplary embodiments, the conditioning agent is bound to a substrate. In various exemplary embodiments the substrate is glass/silica, metal, plastic, nitrocellulose or 30 polymer. In some embodiments, the interfering substances are antibodies, antigens, virus, DNA/RNA, lipids, or proteins. 2 In some exemplary embodiments, the conditioning agent is a metal complex including a metal ion, the metal ion having co-ordination sites for binding to a substrate. In various exemplary embodiments, the conditioning agent includes a binding agent comprising an antibody, a binding domain, a Fab, an SdAb, an antigen, an immunoglobulin or a ligand. In various embodiments, the 5 one or more interfering substances are removed sequentially from the analyte. In yet another exemplary embodiment, the invention comprises an apparatus for use in removing or decreasing interference in an analyte comprising: coating a substrate of the apparatus with a conditioning agent wherein the conditioning agent includes a metal complex including a metal ion, the metal ion having co-ordination sites for binding to a substrate, and one or more 0 members of a binding pair, wherein the apparatus is exposed to the analyte and wherein when the apparatus is separated from the analyte, one or more interfering substances are removed from the analyte without adulterating the analyte or changing its form. In various embodiments, the apparatus comprises a nanoparticle, magnetic bead, glass slide, polymer substrate, nanoarray, collection tube, filter, cuvette, tube, capillary tube, membrane, foil, microfuge tube, vial or a 5 collection container. In these and other embodiments, the substrate comprises glass, silica, a polymer, metal, ceramic, or a combination thereof. In some embodiments, the interfering substances are removed by specific binding to a member of a binding pair. In these and various other embodiments, the binding pair is immobilized on the conditioned substrate. In some embodiments, the member of the binding pair is an antibody, antigen, a Fab, an SdAb, an .0 immunoglobulin, a binding domain, a ligand, biotin, streptavidin. In these embodiments, the interfering substance is an antibody, an antigen, an immunoglobulin, RNA, DNA, a virus, lipid, streptavidin or biotin. In various embodiments, the substrate is conditioned sequentially along a length for removing various interfering substances. These and other features and advantages of the present invention will be set forth or will 25 become more fully apparent in the description that follows and in the appended claims. The features and advantages may be realized and obtained by means of the instruments and combinations particularly pointed out in the appended claims. Furthermore, the features and advantages of the invention may be learned by the practice of the invention or will be apparent from the description, as set forth hereinafter 3 BRIEF DESCRIPTION OF THE DRAWINGS Various exemplary embodiments of the compositions and methods according to the invention will be described in detail, with reference to the following figures wherein: FIG. 1A. Sandwich Assay, Sandwich assay binding of the conjugate and solid phase 5 antibodies to the assay specific antigen. In this Figure, the conjugate antibody is labelled with the Manufacturer/platform-specific chemiluminescent substrate such as acridenium (on left side in Figure 1A), or with a chemiluminescent enzymatic protein such as ALP (on right side in Figure 1A). In the absence of interference, both the solid phase and conjugate antibodies are free to bind the antigen and form a sandwich. Assay dose response is directly proportional to the assay signal 0 response, or number (moles) of sandwiches formed and captured on the solid phase (still bound to solid phase after the final wash and substrate addition). FIG 1B. HAAA Interference and Steric Crowding in a Sandwich Assay; Incorrect sandwich assay binding due to HAAA steric hindrance whereby human IgG and/or IgM bind to the solid phase antibody, conjugate antibody, or both, and sterically crowd the solid phase antibody 5 and/or conjugate antibody so that they cannot freely form a sandwich with the antigen. As assay dose response is directly proportional to the number of sandwiches formed or captured on the solid phase, a failure to form and/or capture the correct number of sandwiches will result in suppressed assay signal and may result in an erroneously low result. FIG IC. Incorrect sandwich assay binding due to HAAA bridging whereby human IgG .0 and/or IgM bind to the solid phase antibody and conjugate antibody forming an antigen independed sandwich. In other words, HAAA mimics the antigen resulting in non-specific capture of the conjugate antibody on the solid phase, or bridging binds the conjugate antibody(s) to the solid phase antibody regardless if either antibody has captured the antigen. As assay dose response is directly proportional to the number of sandwiches formed or captured on the solid phase, bridging 25 will result in elevated assay signal and may result in an erroneously high result. This is the classic "HAMA" interference mechanism. FIG. 2A. Competitive Assay; Competitive Assay binding of the antigen and tracer to the solid phase antibody. In this Figure, the tracer is the antigen (or analogue thereof) conjugated to the Manufacturer/platform-specific chemiluminescent substrate such as acridenium (on left side 4 in Figure 2A), or antigen conjugated to a chemiluminescent enzymatic protein such as ALP (on right side in Figure 2A). In the absence of interference, both the antigen and tracer are free to bind to and compete for the limiting solid phase antibody. Assay signal dose is inversely proportional to the assay signal response, or to the number (moles) of tracer captured on the solid phase (still 5 bound to solid phase after the final wash and substrate addition). FIG 2B. HAAA Interference and Steric Crowding in a Competitive Assay; Incorrect competitive assay binding due to HAAA steric hindrance whereby human IgG and/or IgM bind to the solid phase antibody, tracer, or both, and sterically crowd the solid phase antibody and/or tracer so that they cannot freely bind to eachother. As assay dose response is indirectly proportional to 0 the number of tracers captured on the solid phase, a failure to capture the correct number of tracers will result in suppressed assay signal and may result in an erroneously high result. FIG. 2C. HAAA Interference and Bridging in a Competitive Assay; Incorrect competitive assay binding due to HAAA bridging whereby human IgG and/or IgM binds to the the tracer independed of antigen competition or concentration. In other words, HAAA results in non-specific 5 capture of the tracer on the solid phase. As assay dose response is indirectly proportional to the number of tracers captured on the solid phase, bridging will result in elevated assay signal and may result in an erroneously low result. FIG. 3A. Delayed Capture Assay; Homogeneous solution-based sandwich binding between a tag labelled capture antibody (i.e. a biotin or fluorescene labelled antibody), conjugate .0 antibody (i.e. labelled with a chemiluminescent molecule or enzyme) and the antigen (on left side of Figure 3A), or homogeneous solution-base competitive binding of antigen and tag labelled antigen (i.e. antigen conjugated to biotin or fluorescene) to the conjugate antibody. In the absence of sample specific endogenous interference such as free biotin or free fluorescene from the diet, supplementation, medicine or medical therapy, the solid phase binding protein (i.e. streptavidin, 25 anti-fluorescene antibody) is free to bind the tag labelled sandwich complex as depicted on the left side of Figure 3A, or the solid phase binding protein is free to bind the tag labelled antigen, whether it is free or bound to the conjugate antibody, as depicted in the competitive assay format on right side of Figure 3A. In both cases, assay dose will be accurately reflected by assay signal response where dose is directly proportional to signal in the sandwich delayed capture assay format, but 30 dose will be inversely proportional to signal in the competitive delayed capture assay format. 5 FIG 3B. Endogenous Patient Interference in a Delayed Capture Assay; If there is sample specific endogenous interference present in the patient specimen such as biotin or fluorescene from the patient's diet, supplements, medication, or medical therapy, these interfering substances can bind to the solid phase binding protein if said protein has high specificity or corss-reactivity to the 5 interfering substance. For example, if the patient was eating a diet high in biotin (also known as vitamin H or coaenzyme R), was taking nutritional supplements containing high levels of biotin, and/or was receive medication containing high levels of biotin, their blood, serum or plasma may also contain high levels of biotin. Such a patient, if tested by an assay format employing a delayed streptavidin solid phase .capture assay could result in erroneously high or low results if the free 0 endogenous biotin in the patient sample competes for the streptavidin biotin binding sites, or if the free biotin decreases total streptavidin solid phase biotin binding capacity. If such intererence occurs the streptavidin will not be able to freely bind the biotin labelled sandwich complex or the biotin labelled antigen resulting is suppressed assay signal and a false low dose (sandwich format) or false high dose (competitive format). 5 FIG. 4. Platform Coupling Technology; technology rovides nanometre glus forsorts of surfce Fli. 5. Control of Surface Wettability. FIG. 6: Formation of Nanometer Films. FIG. 7: The invention provides the ability to allow coupling technology on most .0 analytical substrates including microarrays, particles, biosensors, membranes and microtitre plates. FIG. 8: Mix&Go provides easy surface activation and one-step protein coupling. FIG. 9: The invention provides superior protein binding performance compared to market leaders. 25 FIG. 10: The invention provides superior performance for microarrays, both in blocking interference and giving sharper results and pre-blocking of glass array slides. FIG. 11: illustrates the use of the instant invention in increasing the sensitivity of streptavidin assays for both specific and non-specific binding. 6 FIG. 12: illustrates the sensitivity of the Mix&Go system where the size difference of the naked particles compared to activated particles is approximately 2nm (FIG. 12A) but with highly sensitive results in a lateral flow assay system (FIG. 12B). FIG. 13 illustrates the results of a sandwich assay using magnetic particles activated with 5 Mix&Go compared to a commercial competitor. FIG. 14 illustrates the reproducibility of Mix&Go activated particles on binding two or more proteins. FIG. 15 is a cartoon illustrating the benefits of the disclosed system in binding many different types of analytes. 0 FIG. 16 is a cartoon illustrating the benefits of the disclosed system for use on a wide array of substrates. FIG. 17 illustrates some of the benefits of the invention described herein. 5 DETAILED DESCRIPTION OF THE FIGURES It must be noted that as used herein and in the appended claims, the singular forms "a", "an", and "the" include plural reference unless the context clearly dictates otherwise. As well, the terms "a" (or "an"), "one or more" and "at least one" can be used interchangeably herein. It is also .0 to be noted that the terms "comprising", "including", "characterized by" and "having" can be used interchangeably. Unless defined otherwise, all technical and scientific terms used herein have the same meanings as commonly understood by one of ordinary skill in the art to which this invention belongs. All publications and patents specifically mentioned herein are incorporated by reference 25 for all purposes including describing and disclosing the chemicals, instruments, statistical analyses and methodologies which are reported in the publications which might be used in connection with the invention. All references cited in this specification are to be taken as indicative of the level of skill in the art. Nothing herein is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention. 7 While products exist in the market today to troubleshoot heterophile interference in patient specimens such as Heterophilic Blocking Reagent (Scantibodies), Poly MAK 33 (Roche Diagnostics), Immunoglobulin Inhibiting Reagent (Bioreclamation), and Heteroblock (Omega Biologicals), none of these solutions are simple, cheap, or automatable, nor can they address 5 multiple mechanisms of sample specific interference at the same time (i.e. both HAAA and MASI). They consist of manual methods that impact laboratory workflow (WF) and turn around time (TAT), and commercially available blocking reagents are expensive and not feasible for routine clinical use. All blocking reagents sold today are Research Use Only (RUO) and not in vitro diagnostic (IVD) as they are not FDA cleared. They are primarily used to troubleshoot patient 0 results not fitting the clinical picture, or atypically high or low results (i.e. out of range results), but there are many erroneous results today due to HAAA and/or MASI that are transparent to the laboratory and therefore non-obvious to the clinician or laboratory. In fact, these are the most concerning results to lab manager and directors as they can impact patient health and management and ultimately safety and efficacy. 5 IVD Manufacturers are aware of heterophiles and assay specific interference (i.e. specific to a reagent(s) used in their assay construct and design) that may impact the accuracy of results, and they add language to their package inserts/ instructions for use (IFU) accordingly to acknowledge this limitation of use such as the following by Beckman Coulter for their Access .0 250H Vitamin D Total assay: Limitaiona of i. This prout is for use on Unic l 7D xi inassy Sy;tems on1y. It is not comtatible with thne Procedure Access 2 immunoass t 2, eptabe measn rge of the asay is defined as range Lfo th Linit of cetection (Lc'D1 to di Calirt c' .,ue, 220 to approximately 20 ngmL (5.0 t ~25 nm1o/L. Vahue3 oIsid o t hais ralge sho uld bi Feported aI e u 00 ng/mL or > L 5 Caibrator aue (-~110 rgymL , resredivey.h Do nct dilute patient samples, as dus coi lea to mcorect Vitam:in D results. 1 Fcr assays empicymg aniibdies, the posiblty ?xists o r irnc by hetercphile an1b2des n the pa1nt sample. Patients who have been regtdarly expoed to animal; or have reied imm or diagnosuc procedures niz im ng o iunummoglun fragrments maye prdE antibodies e. HAMA, dit inerfere with fimmnunoasays. Additonaym. otw heterophle antbodies (e.g. hu anti-heep antibodies) may be present in ptient sample- £>" Such interfering antibcdies may cause eryroeoUs results. Carefully evahate the rest's tf pns suspected of having these antibodieS, 4. Other potenal interferences in the pae~n sample could. !e presen t t and may cause erroit ous resdt3 in mnrnvassav. SOme ±xamiplEs tha have been documented in literatum indude theumatoid fator endogenous alkin osphse nbim and ptmtems capabLe of binhding to aiphht Carefuly vluae the±oi u ofi a'enz. suspected of havmg these types of mterfees. 8 Similarly, FDA recalls resulting from incorrect diagnostic for many major JVD manufacturers have been made due to results arising from interference. For example, FDA recall number Z-1659-2014 was issued with regard to Siemens ADVIA Centaur Systems Assay because Samples containing fluorescein may show interference with the ADVIA Centaur Systems TSH3 5 Ultra, Vitamin D and the ADVIA Centaur BRAHMS Procalcitonin assays. FDA recall number Z-1654-2014 was issued due to interference with Siemens TSH radioimmunoassay. Sample Interference While there are many sources of sample specific interference in the clinical laboratory such as sample type, cross-reactivity, carry-over, stability, haemolysis, icterus, lipemia, and effects of 0 anticoagulants and sample storage, this project proposal will focus only on mitigating known mechanisms of interference that are difficult to detect in the laboratory, or result is false high or low results such as human anti-animal antibodies (human anti- bovine, goat, mouse, rabbit, and sheep IgG and IgM, and/or rheumatoid factor (RF) interference), and Manufacture assay specific interference such as ABEI, acridenium ester, alkaline phosphates (ALP), bovine serum albumin 5 (BSA), horse radish peroxidase (THRP), ruthenium and streptavidin. Table 1. Primary Failure Modes of Immunoassays Assa speiicttefrec binds to the ass!ay re agent LAbel pevenug~ sub&setvqet bindn to) the Oh phase binding A i t binds 10 th( sd phse binding arer Of bti toS Csltflrv ' ues to) anVt asre 2A ft g t h solid FSure 18 whicrsuks ticas hig dosca bdsndw sa)o as a HAAA regtes se nd ur!A sid phas wi t\cW re suts in fase Ow dose(anwc as'say) or als hg done (opdieasy The assaregnt refeet bmnd antigens conjgteo both" without, steIc ndacbdinorn yescfc 9 Table 1. Describes the primary assay failure modes attributed to human anti-animal antibody (HAAA) interference (Failures 1A and 1), or attributed to Manufacture-specific assay interference (Failures 2A and 2B), that can result in falsely elevated or suppressed 5 assay signal response and erroneous results in sandwich and competitive assay formats: In order to describe the mechanisms for the sample interference failures modes described in Table 1, Figures 1A-IC, 2A-2C, and 3A-3B demonstrate how a sandwich assay format, competitive assay format, and delayed capture assay format, respectively, are impacted by HAAA 0 or MASI interference. In each Figure: * The tracer (conjugate) is either labelled with a small chemiluminescent molecule (i.e. small green circles in Figures) or with a large ch i enzyme (tertiary protein structure looking shape in Figures). Both approaches are used today by Immunoassay 5 Manufacturers. For example, Abbott, IDS, DiaSorin, Roche and Siemens use small chemiluminescent molecules attached to their tracers (acridenium ester, ABEI, ruthenium), while Beckman Coulter and Ortho Clinical Diagnostics use large proteins (ALP, H1RP). * The blue crescent shape represents the assay solid phase. The solid phase can be any surface used in immunoassays such as a microtiter plate well (ELISA), microparticle, colloidal .0 particle or biosensor. * The small orange circles or diamonds represent the antigen or what the assay is trying to capture and measure. * HAAA interference is depicted as either an antibody (purple/red color IgG) or an Immunoglobulin M (purple/red IgM with 5 IgG attached to a central purple circle). 25 e In Figure 3A and 3B, delayed capture is demonstrated with a streptavidin solid phase (blue tetramer shape) and biotin (small grey circles). All immunoassays are susceptible to various sample specific interferences that can result in erroneous test results and lead to unfavourable patient outcomes, there is a need for a simple, inexpensive, automatable but most importantly effective solution to mitigate sample specific 30 interferences and improve the quality of patient results. In the U.S. alone up to 10 billion laboratory tests are performed each year, and the global immunoassay instruments and reagents 10 market is expected to reach $19.1 billion by 2018. Moreover, this same serum depletion approach could be used to develop new solid phase extraction (SPE) products to support the LC-MS/MS diagnostic Market for simple, inexpensive, and automatable serum depletion of target analytes for subsequent elution and analysis by LC-MS/MS, as well as the Molecular Diagnostics Market for 5 sample preanalytical processing and nucleic acid purification and concentration for accurate, reproducible, clinically relevant molecular diagnostics for precision medicine. While Manufacturers do their best to design their assays to mitigate such interference such as adding blocking reagents to the conjugate, beads, and/or assay buffer, assay format/design (1 0 step vs. 2-step vs. delayed addition formats), adding an additional incubation steps and time for sample pre-treatment, and/or decreasing sample volume size, sample specific interference is the inherent weakness of all immunoassays as compared to LC-MS/MS which mitigates such protein based interference due to SPE prior to analysis (i.e. organic extraction and protein precipitation). Since LC-MS/MS and Molecular Diagnostics offer superior specificity and sensitivity as 5 compared against immunoassays (IA), and with recent advancements in SPE, column switching, and analysis, the throughput of these new technologies can now rival some of the fully automated IA analyzers. Many labs have started to implement LCMS for routine testing of small molecules (endocrinology, vitamin D), or molecular testing for infectious disease (ID) even though they prefer the cost savings, and automation offered by the large IA analyzers and track systems. .0 For routine pre-treatment of patient specimens, the pre-analytical product should be automatable and not impact laboratory WF or TAT, nor should it add significant labor or test related costs in the laboratory. Ideally this product would be reimbursed or offered by the immunoassay Manufacturers as a value-add to improve the quality of their assay results. 25 Additionally, this product should give the laboratory complete freedom and flexibility to decide which samples or assays require sample pre-treatment as some labs will want to pre-treat every sample for a specific assay, while others may only be interested in reflex testing or troubleshooting patient results that don't fit the clinical picture. 30 The prevalence of heterophilic interference is both patient and population specific and is estimated to range from 0.1% (1 out of 1,000 patients) to 15% (15 out of 100 patients). While 11 HAAA interference is primarily attributed to human heterophilic antibodies specific to mouse, goat, rabbit, sheep or bovine IgG commonly used in immunoassays, MASI is attributed to patient specific interference directly or indirectly (i.e. antibodies against) from diet, nutritional supplements, medications or medical therapy/treatment that bind or interact with immunoassay 5 critical raw materials. Examples of MASI include: - Abbott Laboratories - acridenium ester - Beckman Coulter - alkaline phosphatase (ALP) - DiaSorin - ABEI (isoluminol) - Ortho Clinical Diagnostics - horse radish peroxide (HRP) 0 - Roche Diagnostics - biotin, ruthenium and streptavidin - Siemens Healthcare - fluorescein, acridenium ester, anti-fluorescein antibody As the prevalence of interference can vary within a population, and between populations, so can the avidity and titer (concentration) of such heterophiles that makes it very difficult for 5 Manufacturers to design around or 100% mitigate such interference mechanism. While they add blockers, or optimize incubation and wash parameters, they can only mitigate interference to a certain extent, and would benefit from sample pre-treatment if possible. Therefore, it is very difficult to impossible for Laboratories to know which specimens in fact have heterophilic interference resulting in falsely elevated or suppressed results in a given assay, from those .0 specimens who do not have interference and result in correct and clinically accurate results. It is only those samples with atypically high or low results (or out of range results) that are currently detected by laboratories, while the majority of interference goes undetected. In fact, since most laboratories work with de-identified patient IDs, nor do they have or review the patient records, they would not know if they are reporting erroneous results unless the physician complains or 25 notifies the lab that a given patient result does not fit the clinical picture. There is a clinical need for both a method(s) and IVD product that can be implemented and automated by the laboratory to mitigate primary mechanisms of heterophilic interference and Manufacture assay-specific interference, improve the accuracy and quality of results reported to 30 physicians, and ultimately to improve the health and well-being of patients. 12 Anteo Diagnostics, the applicant of the instant application, has a novel and patented technology to modify and functionalize a variety of different solid phase surfaces with its metal based chelating methods, tradenamed Mix&GoTMT chemistry for subsequent attachment of highly functional and active proteins. This technology is described U.S. Patents 8,168,445; 5 8,273,403; patent applications 13/410,719; and 13/697,293 each of which is incorporated hereby in its entirety. Other patents and applications describing the Mix&GoM technology are AU2014902315; PCT/AU2005/000966 (WO 2006/002472); PCT/AU2003/000566 (WO 2003/095494); PCT/AU2011/000537 (WO 2011/140590); and PCT/AU2014/050181 (WO 2015/021509) each of which are incorporated herein in their entirety. In addition, Anteo 0 Technologies has developed and commercialized various formulations of Mix&GoM, and Mix&GoTM based products, that are directly applicable to this new and novel serum depletion product line to meet this clinical need: - Mix&GoTM activated paramagnetic microparticles for subsequent attachment of 5 antibodies, proteins or other blocking reagents such as the AMG Coupling Kit 1 [tm Magnetic Particles. These Mix&GoTm formulations and Anteo's expertise can be used to develop magnetic particles coated with specific blocking proteins to bind MASI or HAAA interferences. .0 - Mix&GoTm activated plastics (i.e. polystyrene and CCO) such as microtiter plates and biosensors for subsequent attachment of antibodies, proteins or other blocking reagents such as Mix&GoTM Biosensor or new Mix&GoM formulations such as H14 that can bind to hydrophobic surfaces. These Mix&GoM formulations and Anteo experience can be used to develop sample tubes, plates, filters, membranes, sensors, channels, etc. 25 coated with specific blocking proteins to bind MASI or HAAA interferences. Strategy For the simple, fast, effective, cost beneficial and automated sample pre-treatment in the clinical laboratory, Anteo Technologies can develop and commercialize complementary product 30 lines that can be used independently or together to pre-treat samples and mitigate primary mechanisms of interference: 13 * Mix&GoTM activated secondary sample tubes functionalized with Mix&GoTM and coated with animal antibodies or animal serum to block HAAA, or coated with Manufacturer assay specific reagents such as streptavidin, ALP, HRP, BSA-fluorescein, 5 BSA-ABEI, BSA-acridenium, or BSA-ruthenium to block MASI. There can be a separate Anteo sample tube for each HAAA or MASI mechanism, or sample tubes that address two or more mechanisms either by co-coating blockers on a given sample tube. The advantage of this approach is the sample addition and sample tube mixing can easily be automated on existing sample handling platforms, or via an Anteo developed sample handling instrument 0 via a strategic partnership with a laboratory instrumentation Manufacturer, and the pre treated sample in its specific secondary sample tube can be loaded and tested "as is" on the Manufacturer analyzer as only the targeted interference will be captured and bound (sequestered) to the sample tube's walls, while the supernatant in the sample tube will now be depleted and free of such interference. 5 * Uniform size, 1.0 to 3.0 micron, paramagnetic microparticles, functionalized with Mix&GoTM and coated with HAAA and/or MASI specific blocker(s). There can be separate Anteo particles for each HAAA or MASI mechanism, or particles that address two or more mechanisms either by co-coating blockers on a given particle, or by mixing a 0 plurality of different HAAA and/or MASI serum depletion particles. The advantage of this approach is the addition, mixing, and removal of the magnetic particles can easily be automated on existing sample handling platforms, or via an Anteo developed sample handling instrument. This approach requires magnetic particles with excellent magnetic susceptibility and size uniformity for 100% removal after addition, and good colloidal 25 stability (slow settling rate) to maximize binding kinetics and minimize incubation time needed. Another magnetic particle approach, which is simpler and similar to the secondary sample tube approach, is to design new Manufacturer specific sample racks, or modify existing racks, with magnets to pull the magnetic beads to the sides of the sample tube as only the targeted interference will be captured and bound (sequestered) to the sample tube's 30 walls via the magnetic particles and magnets, while the supernatant in the sample tube will 14 now be depleted and free of such interference as well as depleted and free of the magnetic particles which could interfere in the assay if still present in the sample. " Polystyrene or plastic pins functionalized with Mix&GoTM and coated with HAAA and/or 5 MASI specific blocker(s). There can be a separate pin for each HAAA or MASI mechanism, or pins that address two or more mechanisms by co-coating blockers on a given pin. The advantage of this approach is the pin addition, sample mixing, and pin removal can easily be automated on existing sample handling platforms, or via an Anteo developed sample handling instrument. Also, unlike the sample tubes or magnetic bead 0 approaches the pin is a solid state mass that can be inserted and removed from the sample, and will no longer be present when the sample is loaded and tested on the Manufacturer analyzer. * Filtration plate where the filter membrane or filtration resin is functionalized with 5 Mix&GoTM and coated with HAAA and/or MASI specific blocker(s). There can be a separate plate for each HAAA or MASI mechanism, filtration plates that address two or more mechanisms by co-coating blockers in each well or by coating each row or column of wells with a blocker(s). The advantage of this approach is sample addition and filtration can easily be automated on existing plate handling platforms (vacuum manifold or 0 centrifugation), or via an Anteo developed sample handling. Similar to the pin approach, but also unlike the tubes or magnetic particle approaches, the filtration plate is independent of the sample itself. Once the sample has been filtered (pre-treated) the sample supernatant collected in the collection plate or collection tubes can be loaded and tested on the Manufacturer analyzer, and the filtration plate discarded or regenerated. 25 * It is also possible to consider a primary blood collection sample tube approach strategy using Anteo specific magnetic beads dried/lyophilized in the primary sample tube, Mix&GoT activated and functionalized primary sample tube with subsequent binding of blockers, or a combination of both. The advantage is that the sample gets pre-treated 30 immediately upon blood collection, and interference can already be reduced ahead of time 15 to lessen the burden downstream, or possibly mitigate the need to pre-treat the sample for certain or specific types of known interference (MFG specific). * Point of Care is also a target for sample pre-treatment to mitigate HAAA and MASI. The 5 sample pad, sample filter, sample flow channel(s), and sensor are some of the target surfaces Anteo could functionalize with Mix&Gow to bind blocking reagents. The Anteo Mix&Go' technology can be used to prepare functionalized sample tubes (i.e. secondary sample tubes), as well as paramagnetic particles, for subsequent binding of functionally 0 active blocking reagents for sample pre-treatment to mitigate/remove/eliminate heterophiles (i.e. human anti-mouse IgG, goat IgG, sheep IgG, rabbit IgG, bovine IgG, etc.) and/or Manufacture specific interferences (i.e. free biotin and anti-ruthenium antibodies for Roche, free fluorescein and anti-fluorescein antibodies for Siemens, anti-alkaline phosphatase antibodies for Beckman, etc..) from patient specimens prior to testing these specimens on a given analyzer. 5 * A common HAAA-specific blocking strategy successfully used today by many IVD companies in automated assays/analyzers is species specific serum (i.e. mouse serum for Monoclonal antibodies, goat serum for Goat IgG, etc.) from 1% to 5% (v/V), and/or purified IgG from 0.1% up to 1% (w/v) added to the assay buffer and/or beads. * Serum typically works best as it presents species specific antibodies and proteins in their native conformations and is the most immunogenic/reactive. For this Mix&Go product, Anteo should try coating serum on sample tubes and beads, as well as purified IgG, and look at them separately, as well as at different pooled ratios, for optimal depletion of 25 interference While serum-based species specific blockers work best for HAAA interference, there are other commercially available blockers that we may also want to coat (or co-coat) on sample tubes and bead with Mix&Go such as provided by Scantibodies, or the PolyMAK33 reagent sold by 30 Roche for HAMA and RF interference for monoclonal IgGI, IgG2a and IgG2b based assays. 16 Regarding manufacture specific interference, sample tubes and particles coated with these specific reagents/chemicals used in these assay constructs can be prepared. Since a lot of these sources of interference are small molecules, conjugating them to a carrier protein such as BSA, and different linker strategies and different linker lengths, will be explored based on what the assay 5 conjugate likely used, but also based on steric accessibility by the interfering antibodies and proteins (need to see it to bind it). For example, for ABEI (isoluminol) used in assays by DiaSorin, Inc, could be conjugated to BSA, and bind the BSA-ABEI to the sample tubes and beads via Mix&GoM. The same would 0 be true for fluorescein (Siemens), biotin (Roche), and acridinium ester (Abbott and Siemens). Larger proteins can be directly conjugated such as alkaline phosphatase (Beckman), streptavidin (Roche), and monoclonal anti-fluorescein antibody (Siemens). Automated systems for interference removal/depletion include but are not limited to: 5 * Intuitive software to facilitate ease of use with advanced, automated sample loading and sorting, to minimize manual handling, and conductive tips with graphite fraction mean accurate measurement of filling level 0 Decapping; compatible with rubber stoppers, plastic and screw-style caps, unique 3-D cap color analysis validates sample type against test ordered for error prevention, and detection of newest generation of coded caps * Through-the-label sample volume detection; RTL (Read Through Labels) infrared volume 25 detection up to 3 layers of labels on the sample tube, and Intelligent aliquotting and sample tube labelling to eliminate manual sample preparation errors and ensure faster, more accurate secondary sample tube preparation with "Intelligent" aliquoting transfers the proper volume for samples with single or multiple tests. 30 e Sample bar-code reader ensures positive patient sample identification and notifies the Laboratory Information System (LIS) of sample receipt 17 * Automated measurement of each sample's volume prior to dispensing into aliquot tube or for storage, and automated measurement of plasma or serum volume ascertains whether all aliquots can be created, and computerized prioritization of aliquots ensures most critical 5 samples are created first, if sample volume is minimal, and detects clots and routes samples for manual processing * If necessary, gently mix or vortex the secondary tube (might be necessary if the secondary tube is functionalized with Mix&Gom and coated with blockers, and mixing is required to 0 maximize and improve sample blocking efficiency and to shorten process time) * If necessary, add, mix and remove paramagnetic blocking beads from the secondary tube the instrument could have a reagent bay that could hold different Anteo bead reagents (i.e. Mouse IgG beads, Goat IgG beads, Sheep IgG beads, streptavidin beads, etc.), and based 5 on the barcode information and tests requested of a given sample a single bead type, or a plurality of beads, could be added to a given sample to address assay(s) and/or Manufacturer(s) based interference mechanisms depending on the given assay(s) or analyzer(s) the sample will be tested. 0 The sample in the secondary tube is now pre-treated and ready for testing: the interference(s) will either be depleted and bound to the secondary tube wall, and/or or depleted by binding to the paramagnetic bead(s) and physically removed form the sample with a magnet (such as magnet inside disposable tips whereby the beads collect on the disposable tip and the tip is removed from the sample and discarded). This approach can take advantage of the tube and 25 bead approach to mitigate interference, and would give the lab ultimate flexibility as to which samples to pre-treat, and how to pre-treat the sample using the following 2x2 matrix: 1. NO/NO: No sample pre-treatment - primary tube remains the testing tube, or sample is transferred to a generic secondary tube (common tube used by lab) 30 18 2. YES/NO: Mix&Go Secondary tube pre-treatment - sample is transferred (aspirated and dispensed) into the Mix&Go specific secondary tube 3. NO/YES: Mix&Go bead pre-treatment - sample is transferred to a generic secondary tube 5 (common tube used by lab), and Mix&Go bead(s) are added to the sample, mixed, and removed with magnet 4. YES/YES: Mix& Go Secondary tube + Mix&Go beads pre-treatment - sample is transferred (aspirated and dispensed) into the Mix&Go specific secondary tube, 0 and Mix&Go bead(s) are added to the sample, mixed, and removed with magnet Various exemplary embodiments of devices and compounds as generally described above and methods according to this invention, will be understood more readily by reference to the following examples, which are provided by way of illustration and are not intended to be limiting 5 of the invention in any fashion. EXAMPLE 1: Modification of Surface Parameters as Needed The present invention provides the ability to provide a platform coupling technology to create the surface needed on the surface the user has. As shown in FIG. 4, Mix&Go formulations 0 can control the strength of binding and various surface properties as needed. Example 2: Control of Surface Wettability As shown in FIG. 5, the current invention provides the ability to provide a hydrophobic or hydrophilic surface as needed, where it is needed on a substrate. 25 Example 3: Formation of Nanometer Films As shown in FIG. 6, the instant invention provides the ability to form nanometer films on substrates. Here the substrate is formed on a gold colloid particle. 30 Example 4: Coupling Technology for Most Surfaces 19 The present invention provides the ability to allow coupling technology on most analytical substrates including microarrays, particles, biosensors, membranes and microtitre plates, FIG. 7. Example 5: Surface Activation and Binding Kinetics FIG. 8 illustrates Mix&Go provides easy surface activation and one-step protein coupling. 5 Example 6: Mix&Go Protein Binding Performance As shown in FIG. 9, the invention provides superior protein binding performance compared to market leaders. 0 Example 7: Mix&Go is Superior on Glass Slides As shown in FIG. 10, the invention provides superior performance for microarrays, both in blocking interference and giving sharper results and pre-blocking of glass array slides. EXAMLPLE 8: Mix&Go on Nanoparticles 5 FIG. 11 illustrates the use of the instant invention in increasing the sensitivity of streptavidin assays for both specific and non-specific binding. EXAMPLE 9: Antibody and BSA Co-Coupling on Mix&Go activated Gold Nanoparticles FIG. 12 illustrates the sensitivity of the Mix&Go system where the size difference of the 0 naked particles compared to activated particles is approximately 2nm (FIG. 12A) but with highly sensitive results in a lateral flow assay system (FIG. 12B). EXAMPLE 10: Mix&Go on Magnetic Particles FIG. 13 illustrates the results of a sandwich assay using magnetic particles activated with 25 Mix&Go compared to a commercial competitor. EXAMPLE 11: Co-Coupling & Multi-Functional Constructs As shown in FIG. 14, Mix&Go activated particles can reproducibly bind two or more proteins simultaneously. As shown, individual protein density can be controlled by the amount 30 added even on nanoparticles. 20 While this invention has been described in conjunction with the various exemplary embodiments outlined above, various alternatives, modifications, variations, improvements and/or substantial equivalents, whether known or that are or may be presently unforeseen, may become apparent to those having at least ordinary skill in the art. Accordingly, the exemplary embodiments 5 according to this invention, as set forth above, are intended to be illustrative not limiting. Various changes may be made without departing from the spirit and scope of the invention. therefor3e, the invention is intended to embrace all known or later-developed alternatives, modifications, variations, improvements and/or substantial equivalents of these exemplary embodiments. 0 21