WO1999064864A1 - Optimisation de la sensibilite dans des tests colorimetriques colloidaux en ecoulement continu et en ecoulement lateral - Google Patents

Optimisation de la sensibilite dans des tests colorimetriques colloidaux en ecoulement continu et en ecoulement lateral Download PDF

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Publication number
WO1999064864A1
WO1999064864A1 PCT/US1999/013284 US9913284W WO9964864A1 WO 1999064864 A1 WO1999064864 A1 WO 1999064864A1 US 9913284 W US9913284 W US 9913284W WO 9964864 A1 WO9964864 A1 WO 9964864A1
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WO
WIPO (PCT)
Prior art keywords
colorimetric
immunoassay
site
antibodies
ligand
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Application number
PCT/US1999/013284
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English (en)
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WO1999064864A9 (fr
Inventor
Lawrence Loomis
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New Horizons Diagnostics Inc.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by New Horizons Diagnostics Inc. filed Critical New Horizons Diagnostics Inc.
Priority to AU44390/99A priority Critical patent/AU4439099A/en
Publication of WO1999064864A1 publication Critical patent/WO1999064864A1/fr
Publication of WO1999064864A9 publication Critical patent/WO1999064864A9/fr

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Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
    • G01N33/54313—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals the carrier being characterised by its particulate form
    • G01N33/54346—Nanoparticles
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
    • G01N33/54366—Apparatus specially adapted for solid-phase testing
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/58—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving labelled substances
    • G01N33/585—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving labelled substances with a particulate label, e.g. coloured latex
    • G01N33/587—Nanoparticles

Definitions

  • the present invention discloses a colorimetric immunoassay test system.
  • colloidal gold particle concentration immunoassay to achieve sensitive and selective detection of biological materials.
  • Antibodies specific to the agent of interest are conjugated to colloidal gold particles.
  • Colloidal gold consists of discrete, electron-dense, red- colored particles ranging from 10 ng to 100 ng in diameter with a very high extinction coefficient. When concentrated on solid surfaces, these particles can be visually observed. Labeled antibodies can be easily lyophilized and reconstituted without losing activity or specificity.
  • an immune complex will form between the colloidal gold-labeled detector antibody (Ab) and the antigen (Ag) .
  • the test sample is used to reconstitute a dried colloidal gold labeled antibody and the resulting mixture (antibody and test antigen) ascends chromatographically up a strip that ha been layered with a capture antibody or directly through an antibody coated membrane. The presence of a red stripe or a dot is indicative of a positive test.
  • the test strips contain a positive control to ascertain that the test is working properly.
  • U.S. Patent No. 5,514,602 discloses a method of producing a metal sol reagent containing colloidal metal particles.
  • a metal containing solution is reduced under optimized pH conditions to produce metal sol particles of a preselected size.
  • the particles are coated with a coupling compound, and then bound with at least one selected immunochemically reactive component.
  • Particles having different immunochemical specificities are also mixed to produce reagents having multiple selected immunochemical specificities .
  • U.S. Patent No. 5,384,265 discloses contacting a sample which may contain an analyte with a biomolecuie which is bound to a catalytically active colloidal metal particle, to obtain an analyte-biomolecule-colloidal metal particle complex, separating the analyte-biomolecule-colloidal metal particle complex from the sample, reacting the analyte-biomolecule-colloidal metal particle complex with hydrazine in the presence of lucigenin at a pH of 8 to 11; and detecting light generated by the reaction of the analyte-biomolecule-colloidal metal particle complex in the presence of lucigenin.
  • U.S. Patent No. 5,294,369 discloses a gold sol coated with alkanethiols and alkanethiol derivatives which provide groups on the sol available for the linking of binding moieties such as antibodies, antigens or ligand ⁇ to the gold sol.
  • U.S. Patent No. 5,334,538 discloses a gold sol immunoassay system and device.
  • the gold sol bead is held in a funnel member.
  • Antibodies are associated with the gold sol bead.
  • a second antibody is impregnated on an immunosorbent surface .
  • any antigen already reacted with the first antibody present reacts with the second antibody forming a gold: first antibody: antigen: second antibody: immunosorbent complex.
  • the gold sol acts as the visible label.
  • U.S. Patent No. 5,120,643 discloses a process for immunochromatography with colloidal particles .
  • the method comprises the steps of: contacting a chromatographic medium with the test sample, with the medium comprising at least two reaction sites.
  • the first reaction site comprises a dried solution or a labeled specific binding reagent in the presence of a meta-soluble protein, and a second reaction site comprising an immobilized specific binding reagent in relation to the presence or amount of the analyte in the test sample.
  • the labeled reagent is solubilized and at least a portion of the labeled reagent is transported to the second reaction site, with the binding dependent upon the presence or amount of the analyte in the test sample .
  • the labeled reagent is detected at the second site to determine the presence or amount of the analyte in the test sample.
  • U.S. Patent No. 5,079,172 discloses a method and kit for detecting the presence of antibodies using gold-labeled antibodies.
  • Microspheres coated with an antigen reactive with the first antibody are reacted with the first antibody from serum or other sources.
  • the gold-labeled antibody is reacted with the first antibody antigen complex on the microsphere and detected.
  • the gold particles are detected using an electron microscope .
  • PCT/US95/04547 describes the use of soluble submicron particles (dendrimers) that are labeled with antibodies to coat membranes.
  • the assay procedures described are flow through EIA and fluorescence immunoassay ⁇ requiring washing steps in order to obtain a response .
  • the present invention proposes a much more sensitive immunoassay test, which is easier to use and interpret.
  • the entire test is conducted on a test strip, and the detection antibody is preferably a FAB fragment that has been labeled with a 50 - 100 nm gold particle and immobilized on a test pad.
  • the invention provides a simplified, sensitive and specific test procedure for the determination and detection of an immunologically reactive analyte in an aqueous sample .
  • the present invention discloses a capture membrane to align and secure capture antibodies on a solid surface so that the immunological activity of the capture antibody is not sterically hindered. Consequently, optimal binding capacity is achieved, resulting in a minimum loss in binding activity between the capture antibody and the ligand.
  • dendrimers are used to secure the capture antibodies to a test strip upon which a sample is placed.
  • the site of the capture membrane is protein A or protein G.
  • the capture membrane site may be lectin receptors, to which no capture antibodies are applied.
  • Antispecie ⁇ antibodies may be used, particularly in combination with the dendrimers or protein G.
  • the present invention also discloses an improved gold immunoassay test system which uses larger gold colloids for tagging antibodies (anywhere between 50 nm to 100 nm) to increase the sensitivity of test results, (i.e. each specific antibody that reacts, delivers more gold complex to the antibody capture membrane) without any residual non-specific activity.
  • the elimination of non-specific background activity problems results from the use of blocking chemistries which inhibit non-specific reactions without altering the desired specific reaction and the use of specifically designed recombinant FAB antibodies.
  • FAB antibodies are unlike whole antibodies in that their FC or constant regions are eliminated. It is this region of the antibody molecule that often causes problems with non-specificity.
  • the FAB antibodies for detecting a positive result are attached to gold colloidal masses, in the range of 50- 100 nm. These gold-FAB antibody complexes are positioned on a test strip, downstream from where the antigenic sample is applied.
  • the gold FAB-antibodies may be attached to microspheres, thereby allowing for more antibodies to be located at the reagent site.
  • a set of antibodies Further downstream from both the antigenic or ligand sample and the gold-FAB sample is a set of antibodies, specific for the gold-FAB antibody-antigen or an ibody-ligand complex. These antibodies serve to concentrate the complex in one location, thereby allowing for a red stripe to appear on a set section of the test strip when there is a positive reaction.
  • the capture antibodies are located further downstream from the reagent and the sample site.
  • Dendrimers are one way of attaching the capture antibodies to the test strip. Dendrimers are three dimensional, tree-like polymers. The dendrimers have a small size, good solubility, higher segmental densities, interior void space, and lower viscosities. Dendritic polymers can be constructed by both divergent and convergent synthetic methods . The divergent synthesis starts from a center core, and then grows each layer in a stepwise fashion, while the convergent method assembles exterior end groups and dendrons first before being coupled onto a core. Each re-iteration or layer is defined as a generation. The more layers there are in the dendrimeric structure, the more rigid the dendrimers molecule itself becomes.
  • Dendrimers have the advantage, that they can be synthesized with an exactly uniform molecular weight, whereas the conventional polymers always have a particular molecular weight distribution. In dendrimers with particular functinal groups can be manufactured with a defined number of such reactive groups.
  • dendrimers for example polyamidoamine [PAMAMS] dendrimers
  • PAMAMS polyamidoamine
  • the exterior reactive surface groups are the key for linking dendrimers covalently with antibodies as well as providing adhesion onto the surface of a membrane.
  • the structural composition of the dendrimer controls the spatial arrangement of the attached antibody molecules . This assures the optimal binding activity of the immobilized capture antibody.
  • FIG. 1 is an overall view of the immunoassay test system,-
  • FIG. 2 is an exploded view of the immunoassay test system
  • FIG. 3 is a side view of the immunoassay test strip
  • FIG. 4 is an overhead view of the immunoassay test strip
  • Fig. 5 is a schematic drawing of the antigenic-antibody reaction.
  • the immunoassay test system 1 comprises an enclosure 2, which is preferably plastic.
  • This plastic enclosure comprises a top section 3 and a bottom section 4 which are held together by male 5 and female 6 peg joints.
  • the top section 3 of the enclosure 2 has an opening 7 for placing a sample. There is also an opening 8 to visualize the test results 9 and the control results 10.
  • the bottom section 4 comprises a tray 11 into which fits a test strip 12.
  • the test strip 12 preferably has a membrane support 13.
  • the membrane support 13 may be comprised of plastic, cardboard, or any other rigid material .
  • a testing layer 14 preferably made out of nitrocellulose.
  • the nitrocellulose or testing layer 14 are the areas to which the appropriate reagents or samples are applied or affixed.
  • the nitrocellulose/testing layer is affixed to the membrane support 13 by an adhesive 31.
  • sample site 15 At one end of the test strip 12 is the sample site 15 to which the sample is to be applied.
  • This sample site 15 may have another nitrocellulose or adsorbent sample pad 23 residing on top of the testing layer, to which the sample is transferred.
  • the sample may be in the form of an antigen or ligand 16 in a fluid.
  • target ligands and anti-ligands which potentially may be detected or determined includes antigens and ligands found in animal body fluids, as well as antigens associated with bacteria, parasites, fungi, viruses, toxins, anthrax, etc.
  • therapeutic drugs and controlled substances having small molecules, such as, for example, theophylline may be detected or determined using the present invention.
  • the sample travels downstream from the sample site 15 to the gold immunoassay site 18 where FAB antibody coated gold sol particles 19 reside.
  • the gold particles 19 attached to the FAB antibodies 20 are preferably larger than 20 nm, more preferably in the range of about 50 to 100 nm, and most preferably in the range of from about 70 to 90 nm. Larger particles may also be used wherein a number of FAB antibodies 20 are attached to the gold particle 19.
  • the gold sol labeled FAB antibodies 21 are dried and deposited on the strip 12.
  • the metal sol particles to be used in accordance with the present invention may be prepared by coupling an immunologically reactive substance directly to the gold particle.
  • the labeled component may be prepared by coupling the substance to the particle using a biotin/avidin linkage.
  • the substance may be biotinylated and the metal containing particle coated with an avidin compound. The biotin on the substance may then be reacted with the avidin compound on the particle to couple the substance and the particle together.
  • the labeled component may be prepared by coupling the substance antibody to a carrier such as bovine serum albumin (BSA) , and using this to bind to the metal particles.
  • BSA bovine serum albumin
  • the metal sol particles to be used in accordance with the present invention may be prepared by methodology which is well known. For instance, the preparation of gold sol particles is disclosed in an article by G. Frens, Nature, 241, 20-22 (1973).
  • the metal sol particles may be metal or metal compounds or polymer nuclei coated with metals or metal compounds, as described in U.S. Pat No. 4,313,734. Other methods well known in the art may be used to attach the gold particles to the FAB antibodies.
  • the metal sol particles may be made of platinum, gold, silver, or copper or any number of metal compounds which exhibit characteristic colors.
  • the antibodies do not necessarily have to be attached to a metal sol particle, but may instead be attached to a dye with an extinction coefficient equal to or greater than gold.
  • the metal sol particles or dyes should have a high extinction coefficient equal to or greater than gold.
  • the gold labeled FAB antibodies are deposited and dried on a rectangular or square or adsorbent FAB antibody pad 22, the pad preferably about .25" x
  • This FAB antibody pad 22 is positioned downstream from where the sample is applied on the strip 12. Preferably, the FAB antibody pad 22 fits underneath the distal end 24 of the sample pad
  • the antibodies are attached to microspheres. This has the effect of increasing the number antibodies in a given area.
  • the process for attaching the antibodies to the microsphere(s) begins with the use of protein reactive microspheres (MX- Covaspheres* of diameter .5 micrometers or .9 micrometers purchased from Duke Scientific Corporation, Pal Alto, California 94303.
  • the microspheres may also be purchased from other suppliers, as well) .
  • the binding is at the amino groups of the protein. They were then coated with various antibodies.
  • a suspension of the spheres are mixed after sonication with the antibodies in water or in a phosphate buffer solution, after which they are incubated at room temperature for 10-75 minutes.
  • the mixture is then centrifuged in an Eppendorf microcentrifuge and the pellets containing the antibody-linked microspheres are suspended in a buffer containing 1-5% by wt/volume bovine serum albumin (BSA) for 1 hour at room temperature.
  • BSA bovine serum albumin
  • the BSA blocked any unreacted surfaces of the microspheres. After one more centrifugation, at 10,000 for 10 minutes, the spheres were resuspended in the above buffer (TBS with 5% BSA) and stored at 4 degrees C. before using.
  • the solid phase particles may comprise any one of known, water dispersable particles, such as, for example, the polystyrene latex particles discloses in U.S. Patent No. 3,088,875. Such solid phase materials simply consist of suspensions of small, water-insoluble particles to which antibodies are able to bind. Suitable solid phase particles are also disclosed, for example, in U.S. Patent Nos. 4,184,849; 4,486,530; and 4 , 636 , 479.
  • the solid phase particles useful in connection with the invention may comprise, for example, particles of latex or of other support materials such as silica, agarose, glass, polyacrylamides, polymethyl methacrylates, carboxylate modified latex and Sepharose.
  • the particles will vary in size from about 0.2 microns to about 10 microns.
  • useful commercially available materials include .99 micron carboxylate modified latex, cyanogen bromide activated Sepharose beads (Sigma) , fused silica particles (Ciba Coming, lot #6) , isothiocyanate glass (Sigma) , Reactogel 25DF (Pierce) and Polybead - carboxylate monodisperse microspheres.
  • such particles may be coated with a layer of FAB antibodies coupled thereto in a manner known per se in the art to present the solid phase component.
  • the sample contains an antigen or ligand 16 to which the gold FAB antibodies 21 react, there is a antigenic-antibody bonding between the sample and the gold FAB antibodies 21.
  • FAB antibody complex 25 continues to migrate along the capture site
  • the antibodies 27 supported by the dendrimers 32 are designed to react specifically to the antigen, effectively forming an antibody-antigen-gold FAB antibody sandwich 29 if there is a positive reaction. If there is a negative reaction, no "sandwich" is formed, and the unreacted ligand proceeds to the end of the strip 12 wherein an absorbent pad 30 absorbs the fluid and unreacted labelled-antibody proceeds to the end of the strip 12.
  • antibodies are bound to dendrimers prior to their placement on the strip 12. This is then layered on the strip and dried.
  • the antigens or ligaiidfe will attach to the gold FAB antibodies as it migrates from the sample site, whereupon the antigens or ligands will attach to the antibodies attached to the dendrimers. At thie point, the concentrated appearance of the gold particles appears as a red to purple line. If however, the ligands do not attach to the gold labeled antibodies, the antibodies will not be bound to the capture ssiitte 2 ⁇ .
  • Staphylococcus cell wall may be deposited by conventional means to _. the test strip. Because of the -unique chemistry of Protein A and/or ⁇ ** ⁇ *" Protein G, the capture antibodies laid down at the capture site are S shield(vt'e aligned such that the active or binding ends are facing outward from S***" « *
  • a specie ⁇ -antispecies ⁇ *y AJH-I antibody combination Is laid down on the te3t strip.
  • a goat antirabbit antibody is laid down on the test strip.
  • the rabbit antibody is attached or bound to the goat anti-rabbit antibody.
  • the rabbit antibody may be non-specific, so that any antigen that migrates along the test strip will r>e captured by the rabbit antibody. If the colorimetric tagged antibody ia attached to the antigen, a positive result will be appear in the form of an indicator line.
  • the anti-species antibody may be attached to the test strip by a dendrimeric arrangement.
  • the capture site is to have lectin receptors.
  • This lectin layer will bind the antigen as it migrates along the length of the test strip.
  • the lectin may be bound to a dendrimer to optimize its binding capability.
  • the superior sensitivity of this test format allows for detection of amounts of antigen or ligand, measured in picograms .
  • this test can also have positive and negative control lines.
  • the positive control line has an anti-Fab substance or antibody laid down at the appropriate spot on the strip, downstream from the sample test site and from the FAB reagent site. This line should always appear when FAB antibodies are used in the test. If the positive control is negative, then the test is invalid.
  • the negative control can use any nonrelated antibody to coat the strip. There should be no capture of the antigen or ligand by the non-related antibody. If the negative control is positive, i.e., a line appears, than the test is invalid.

Abstract

L'invention concerne un dispositif de test par dosage immunologique qui permet d'identifier facilement des réactions positives. Grâce à ce dispositif de test, on obtient une procédure d'essai simplifiée, sensible et spécifique permettant de déterminer et de détecter un analyte réactif du point de vue immunologique dans un échantillon aqueux. Ce concerne dispositif de test comporte une enceinte plastique (2) pourvue d'une partie supérieure (3) et d'une partie inférieure (4). La partie supérieure (3) de l'enceinte (2) présente une ouverture (7) destinée à recevoir des échantillons et une ouverture (8) destinée à visualiser les résultats des tests (9) et un résultat de contrôle (10). La partie inférieure (4) comporte un plateau (11) dans lequel vient se loger une membrane de capture (12). Celle-ci aligne un anticorps de capture sur une surface solide, de manière que la capacité de capture de l'anticorps ne soit pas gênée par un encombrement stérique.
PCT/US1999/013284 1998-06-12 1999-06-11 Optimisation de la sensibilite dans des tests colorimetriques colloidaux en ecoulement continu et en ecoulement lateral WO1999064864A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AU44390/99A AU4439099A (en) 1998-06-12 1999-06-11 Optimizing sensitivity in colloidal colorimetric flow through and lateral flow tests

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US9650998A 1998-06-12 1998-06-12
US09/096,509 1998-06-12

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WO1999064864A1 true WO1999064864A1 (fr) 1999-12-16
WO1999064864A9 WO1999064864A9 (fr) 2000-03-23

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Cited By (23)

* Cited by examiner, † Cited by third party
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EP1341934A2 (fr) * 2000-12-12 2003-09-10 Autogenomics, Inc. Puce a adn amelioree
WO2005057215A1 (fr) * 2003-11-21 2005-06-23 Kimberly-Clark Worldwide, Inc. Dispositifs d'analyse a ecoulement lateral a membranes faisant appel a une detection par phosphorescence
US7094528B2 (en) 2004-06-30 2006-08-22 Kimberly-Clark Worldwide, Inc. Magnetic enzyme detection techniques
US7651841B2 (en) 2001-12-24 2010-01-26 Kimberly-Clark Worldwide, Inc. Polyelectrolytic internal calibration system of a flow-through assay
US7662643B2 (en) 2002-12-19 2010-02-16 Kimberly-Clark Worldwide, Inc. Reduction of the hook effect in membrane-based assay devices
US7670786B2 (en) 2002-08-27 2010-03-02 Kimberly-Clark Worldwide, Inc. Membrane-based assay devices
US7713748B2 (en) 2003-11-21 2010-05-11 Kimberly-Clark Worldwide, Inc. Method of reducing the sensitivity of assay devices
US7781172B2 (en) 2003-11-21 2010-08-24 Kimberly-Clark Worldwide, Inc. Method for extending the dynamic detection range of assay devices
US7829328B2 (en) 2003-04-03 2010-11-09 Kimberly-Clark Worldwide, Inc. Assay devices that utilize hollow particles
US7851209B2 (en) 2003-04-03 2010-12-14 Kimberly-Clark Worldwide, Inc. Reduction of the hook effect in assay devices
US7906276B2 (en) 2004-06-30 2011-03-15 Kimberly-Clark Worldwide, Inc. Enzymatic detection techniques
US7943395B2 (en) 2003-11-21 2011-05-17 Kimberly-Clark Worldwide, Inc. Extension of the dynamic detection range of assay devices
US7943089B2 (en) 2003-12-19 2011-05-17 Kimberly-Clark Worldwide, Inc. Laminated assay devices
US7964340B2 (en) 2004-06-30 2011-06-21 Kimberly-Clark Worldwide, Inc. One-step enzymatic and amine detection technique
US8137985B2 (en) 2001-12-24 2012-03-20 Kimberly-Clark Worldwide, Inc. Polyelectrolytic internal calibration system of a flow-through assay
US8173383B2 (en) 2005-12-06 2012-05-08 Inbios International, Inc. Methods and materials for the detection of Leishmania infection
CN102590517A (zh) * 2012-01-19 2012-07-18 南京基蛋生物科技有限公司 一种免疫层析试纸及其制备方法
CN106248931A (zh) * 2016-08-08 2016-12-21 武汉中科志康生物科技有限公司 一种抗生素及基于该抗生素的细菌快速层析检测卡
CN106290841A (zh) * 2015-05-13 2017-01-04 上海凯创生物技术有限公司 霍乱弧菌o1乳胶法检测试剂盒
CN106290844A (zh) * 2015-05-13 2017-01-04 上海凯创生物技术有限公司 伤寒杆菌胶体金法检测试剂盒
CN106290842A (zh) * 2015-05-13 2017-01-04 上海凯创生物技术有限公司 霍乱弧菌o139胶体金法检测试剂盒
CN107167602A (zh) * 2017-05-09 2017-09-15 中国疾病预防控制中心传染病预防控制所 多交叉恒温扩增结合金纳米生物传感检测霍乱弧菌的方法
EP3165923A4 (fr) * 2014-07-01 2017-11-29 Nippon Steel & Sumikin Chemical Co., Ltd. Marqueur, méthode de dosage immunologique, réactif de dosage immunologique, méthode de dosage d'analyte, kit de dosage d'analyte, et bandelette réactive pour chromatographie à écoulement latéral

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Cited By (29)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP1341934A4 (fr) * 2000-12-12 2005-04-06 Autogenomics Inc Puce a adn amelioree
EP1341934A2 (fr) * 2000-12-12 2003-09-10 Autogenomics, Inc. Puce a adn amelioree
US7651841B2 (en) 2001-12-24 2010-01-26 Kimberly-Clark Worldwide, Inc. Polyelectrolytic internal calibration system of a flow-through assay
US8137985B2 (en) 2001-12-24 2012-03-20 Kimberly-Clark Worldwide, Inc. Polyelectrolytic internal calibration system of a flow-through assay
US7670786B2 (en) 2002-08-27 2010-03-02 Kimberly-Clark Worldwide, Inc. Membrane-based assay devices
US7662643B2 (en) 2002-12-19 2010-02-16 Kimberly-Clark Worldwide, Inc. Reduction of the hook effect in membrane-based assay devices
US7829328B2 (en) 2003-04-03 2010-11-09 Kimberly-Clark Worldwide, Inc. Assay devices that utilize hollow particles
US7851209B2 (en) 2003-04-03 2010-12-14 Kimberly-Clark Worldwide, Inc. Reduction of the hook effect in assay devices
US8034397B2 (en) 2003-04-03 2011-10-11 Kimberly-Clark Worldwide, Inc. Methods of making assay devices utilizing hollow particles
WO2005057215A1 (fr) * 2003-11-21 2005-06-23 Kimberly-Clark Worldwide, Inc. Dispositifs d'analyse a ecoulement lateral a membranes faisant appel a une detection par phosphorescence
US7713748B2 (en) 2003-11-21 2010-05-11 Kimberly-Clark Worldwide, Inc. Method of reducing the sensitivity of assay devices
US7781172B2 (en) 2003-11-21 2010-08-24 Kimberly-Clark Worldwide, Inc. Method for extending the dynamic detection range of assay devices
US7943395B2 (en) 2003-11-21 2011-05-17 Kimberly-Clark Worldwide, Inc. Extension of the dynamic detection range of assay devices
US7943089B2 (en) 2003-12-19 2011-05-17 Kimberly-Clark Worldwide, Inc. Laminated assay devices
US7964340B2 (en) 2004-06-30 2011-06-21 Kimberly-Clark Worldwide, Inc. One-step enzymatic and amine detection technique
US7094528B2 (en) 2004-06-30 2006-08-22 Kimberly-Clark Worldwide, Inc. Magnetic enzyme detection techniques
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