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Journal articles on the topic 'Microarray immunoassay'

Author: Grafiati

Published: 2 June 2025

Last updated: 31 July 2025

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1

Han, Dongsik, and Je-Kyun Park. "Microarray-integrated optoelectrofluidic immunoassay system." Biomicrofluidics 10, no. 3 (2016): 034106. http://dx.doi.org/10.1063/1.4950787.

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2

Uenoyama, Yuta, Atsushi Matsuda, Kazune Ohashi, et al. "Development and Evaluation of a Robust Sandwich Immunoassay System Detecting Serum WFA-Reactive IgA1 for Diagnosis of IgA Nephropathy." International Journal of Molecular Sciences 23, no. 9 (2022): 5165. http://dx.doi.org/10.3390/ijms23095165.

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Aberrant glycosylation of IgA1 is involved in the development of IgA nephropathy (IgAN). There are many reports of IgAN markers focusing on the glycoform of IgA1. None have been clinically applied as a routine test. In this study, we established an automated sandwich immunoassay system for detecting aberrant glycosylated IgA1, using Wisteria floribunda agglutinin (WFA) and anti-IgA1 monoclonal antibody. The diagnostic performance as an IgAN marker was evaluated. The usefulness of WFA for immunoassays was investigated by lectin microarray. A reliable standard for quantitative immunoassay measur

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3

Shao, Weiping, Zhimin Zhou, Isabelle Laroche, et al. "Optimization of Rolling-Circle Amplified Protein Microarrays for Multiplexed Protein Profiling." Journal of Biomedicine and Biotechnology 2003, no. 5 (2003): 299–307. http://dx.doi.org/10.1155/s1110724303209268.

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Protein microarray-based approaches are increasingly being used in research and clinical applications to either profile the expression of proteins or screen molecular interactions. The development of high-throughput, sensitive, convenient, and cost-effective formats for detecting proteins is a necessity for the effective advancement of understanding disease processes. In this paper, we describe the generation of highly multiplexed, antibody-based, specific, and sensitive protein microarrays coupled with rolling-circle signal amplification (RCA) technology. A total of 150 cytokines were simulta

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Rafique, Saima, Farukh Kiyani, Sumbal Jawaid, et al. "Reusable, Noninvasive, and Sensitive Fluorescence Enhanced ZnO-Nanorod-Based Microarrays for Quantitative Detection of AFP in Human Serum." BioMed Research International 2021 (July 15, 2021): 1–11. http://dx.doi.org/10.1155/2021/9916909.

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The fabrication of sensitive protein microarrays such as PCR used in DNA microarray is challenging due to lack of signal amplification. The development of microarrays is utilized to improve the sensitivity and limitations of detection towards primal cancer detection. The sensitivity is enhanced by the use of ZnO-nanorods and is investigated as a substrate which enhance the florescent signal to diagnose the hepatocellular carcinoma (HCC) at early stages. The substrate for deposition of ZnO-nanorods is prepared by the conventional chemical bath deposition method. The resultant highly dense ZnO-n

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Zhang, Daxiao, Wei Dai, Huatian Hu, et al. "Controlling the immobilization process of an optically enhanced protein microarray for highly reproducible immunoassay." Nanoscale 13, no. 7 (2021): 4269–77. http://dx.doi.org/10.1039/d0nr08407g.

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6

Song, Yujing, Jingyang Zhao, Tao Cai, et al. "Machine learning-based cytokine microarray digital immunoassay analysis." Biosensors and Bioelectronics 180 (May 2021): 113088. http://dx.doi.org/10.1016/j.bios.2021.113088.

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7

Silzel, John W., Bibijana Cercek, Charles Dodson, Tsong Tsay, and Robert J. Obremski. "Mass-sensing, multianalyte microarray immunoassay with imaging detection." Clinical Chemistry 44, no. 9 (1998): 2036–43. http://dx.doi.org/10.1093/clinchem/44.9.2036.

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Abstract Miniaturization of ligand binding assays may reduce costs by decreasing reagent consumption, but it is less apparent that miniaturized assays can simultaneously exceed the sensitivity of macroscopic techniques by analyte “harvesting” to exploit the total analyte mass available in a sample. Capture reagents (avidin or antibodies) immobilized in 200-μm diameter zones are shown to substantially deplete analyte from a liquid sample during a 1–3-h incubation, and the assays that result sense the total analyte mass in a sample rather than its concentration. Detection of as few as 105 molecu

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8

Anderson, George P., and Chris R. Taitt. "Suspension Microarray Immunoassay Signal Amplification Using Multilayer Formation." Sensor Letters 6, no. 1 (2008): 213–18. http://dx.doi.org/10.1166/sl.2008.018.

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9

Päkkilä, Henna, Minna Ylihärsilä, Satu Lahtinen, et al. "Quantitative Multianalyte Microarray Immunoassay Utilizing Upconverting Phosphor Technology." Analytical Chemistry 84, no. 20 (2012): 8628–34. http://dx.doi.org/10.1021/ac301719p.

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10

Lee, Jonghwan, Jaeyeon Jung, Subeom Park, Jie Chen, Jaeyoo Choi, and Jinho Hyun. "Microarray of stimuli-responsive microbeads for duplexed immunoassay." BioChip Journal 5, no. 2 (2011): 158–64. http://dx.doi.org/10.1007/s13206-011-5209-x.

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11

Chang, Yaw-Jen, Hong-Wei Yang, Len-Hao Yao, and Wen-Tung Yang. "Droplet-Based Immunosensor for Simultaneous Immunoassays of Multiplex Histidine-Tagged Proteins." SLAS TECHNOLOGY: Translating Life Sciences Innovation 25, no. 2 (2019): 132–39. http://dx.doi.org/10.1177/2472630319879647.

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This paper presents a droplet-based immunoassay chip allowing each droplet to be positioned in a passive droplet-positioning cavern under continuous flow. In addition, the chip surface can immobilize any kind of histidine-tagged capture agents for performing simultaneous multiplex immunoassays. Distinct families of monodispersed droplets were generated since a diaphragm, which is a thin elastomeric flap film suspended from the top of the main channel, forms a double T junction for shearing the aqueous liquids by the carrier flow. These two types of monodispersed droplets traverse the main chan

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12

Preda, Mariana, Florin-Dan Popescu, Emilia Vassilopoulou, and Sylwia Smolinska. "Allergenic Biomarkers in the Molecular Diagnosis of IgE-Mediated Wheat Allergy." International Journal of Molecular Sciences 25, no. 15 (2024): 8210. http://dx.doi.org/10.3390/ijms25158210.

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IgE-mediated wheat allergy can take on various forms, including childhood food allergy to wheat, wheat-dependent exercise-induced anaphylaxis in young adults, baker’s respiratory allergy/asthma in workers exposed to wheat flour inhalation, and contact urticaria that is caused by hydrolyzed wheat proteins in some cosmetics, and that is sometimes associated with a food allergy. Singleplex and multiplex immunoassays detect specific IgE antibodies to wheat allergenic molecular biomarkers such as omega-5 gliadin Tri a 19, lipid transfer protein Tri a 14, and alpha-amylase inhibitors. The fluorescen

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13

Sauer, G., N. Schneiderhahn-Marra, M. Bãuerle, et al. "Protein multiplex sandwich immunoassay: A reliable and objective method for complete molecular characterization of breast cancer from core needle biopsies." Journal of Clinical Oncology 24, no. 18_suppl (2006): 20025. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.20025.

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20025 Background: Within the last years, protein microarrays have been developed to quantify a large number of parameters present in a given sample simultaneously. Such miniaturised and parallelised sandwich immunoassays are of general interest for all proteomic and diagnostic approaches in which several parameters have to be determined from small samples. We describe the development of a bead-based flow cytometry that represents a convenient approach for rapid multiplex detection of functional target molecules from breast cancer biopsies. Methods: Briefly, sonographically guided core needle b

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14

Nadler, Timothy K., Christine Rauh-Adelmann, Cheryl Murphy, et al. "Profiling Protein Tyrosine Phosphorylation: A Quantitative 45-Plex Peptide-Based Immunoassay." Journal of Biomolecular Screening 13, no. 7 (2008): 626–37. http://dx.doi.org/10.1177/1087057108319978.

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Cellular homeostasis and responses to stimuli are mediated by complex signaling network events dominated by changes in protein phosphorylation states. Understanding information flow in the network is essential for correlating signaling changes to cell physiology. Tyrosine phosphorylation constitutes only a small portion of all protein phosphorylation, but its importance is manifested by the significant role it plays in diseases such as cancer. A peptide-based immunoassay microarray, designed to provide site specificity, quantification, broad coverage, and accessibility, is described that profi

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15

Li, Li, Shuai Ren, Manyu Shao, Sarah De Saeger, Suquan Song, and Liping Yan. "A competitive immunoassay for zearalenone with integrated poly(dimethysiloxane) based microarray assay." Analytical Methods 10, no. 33 (2018): 4036–43. http://dx.doi.org/10.1039/c8ay01307a.

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16

Delehanty, James B., and Frances S. Ligler. "A Microarray Immunoassay for Simultaneous Detection of Proteins and Bacteria." Analytical Chemistry 74, no. 21 (2002): 5681–87. http://dx.doi.org/10.1021/ac025631l.

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17

Jain, Bharti, Savita Kulkarni, Sharmila Banerjee, and M. G. Ramakrishna Rajan. "Microarray immunoassay for thyrotropin on track-etched membranes using radiotracers." Journal of Radioanalytical and Nuclear Chemistry 322, no. 1 (2019): 99–104. http://dx.doi.org/10.1007/s10967-019-06507-8.

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18

Liu, Yingshuai, Yuanyuan Zhang, Zhisong Lu, and Chang Ming Li. "3-D microarray and its microfabrication-free fluidic immunoassay device." Analytica Chimica Acta 889 (August 2015): 187–93. http://dx.doi.org/10.1016/j.aca.2015.07.044.

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19

Cui, Yubao, Feixiang Teng, LiLi Yu, et al. "Sequential epitopes ofDermatophagoides farinaeallergens identified using peptide microarray-based immunoassay." IUBMB Life 68, no. 10 (2016): 792–98. http://dx.doi.org/10.1002/iub.1540.

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20

Knight, Paul R., Arun Sreekumar, Javed Siddiqui, et al. "Development of a Sensitive Microarray Immunoassay and Comparison With Standard Enzyme-Linked Immunoassay for Cytokine Analysis." Shock 21, no. 1 (2004): 26–30. http://dx.doi.org/10.1097/01.shk.0000101668.49265.19.

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21

Bijlsma, D., E. Lukasik, M. Hausmann, G. Gomez, C. Ginocchio, and E. Moreau. "AB1552 PERFORMANCE OF A SOLID-PHASE PHOTOMETRIC SINGLE USE IMMUNOASSAY MICROARRAY PROTOTYPE IN THE DETECTION OF IGG ANTIBODIES AGAINST CENTROMERE PROTEIN B (CENP-B) IN HUMAN SERUM." Annals of the Rheumatic Diseases 82, Suppl 1 (2023): 2009.2–2010. http://dx.doi.org/10.1136/annrheumdis-2023-eular.3975.

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BackgroundSystemic Sclerosis (SSc) is a chronic multisystem autoimmune (AI) disease, characterized by progressive fibrosis of the skin and internal organs and vascular injury.[1]Biomarker testing plays an important part in disease classification, identification of sub-sets of SSc (e.g., CREST/ Limited SSc), prognosis and progression. Presence of antibodies against centromere proteins (CENP) weighs 3 points in the ACR/EULAR Classification Criteria.[2]Development of highly automated diagnostic tools remains a clinical need.ObjectivesTo evaluate the performance of a solid-phase photometric single

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22

Jentz, Tim, Wendy Nelson, and Gary Opperman. "Tools for enhancement of diagnostic immunoassay applications (65.42)." Journal of Immunology 186, no. 1_Supplement (2011): 65.42. http://dx.doi.org/10.4049/jimmunol.186.supp.65.42.

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Abstract Optimization of immunoassay applications is often hampered by issues such as non-specific binding, matrix interferences, destabilization of antibody/antigen interactions, and limited sensitivity. SurModics offers tools to address these problems and provides the framework to develop sensitive, reproducible, and robust immunoassays. Stabilization of antibody-protein interactions is fundamental for achieving a robust and reproducible assay. Novel stabilizer formulations have been developed to provide protein stability in both the dried state as well as in solution. The data presented her

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23

Langer, Veronika, Reinhard Niessner, and Michael Seidel. "Stopped-flow microarray immunoassay for detection of viable E. coli by use of chemiluminescence flow-through microarrays." Analytical and Bioanalytical Chemistry 399, no. 3 (2010): 1041–50. http://dx.doi.org/10.1007/s00216-010-4414-0.

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24

Wu, Min, Haidong Liu, Zhaobo Liu, Chao Liu, Aiying Zhang, and Ning Li. "Analysis of serum alpha-fetoprotein (AFP) and AFP-L3 levels by protein microarray." Journal of International Medical Research 46, no. 10 (2018): 4297–305. http://dx.doi.org/10.1177/0300060518789304.

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Objectives This study aimed to examine a simple, effective, time-saving, and low-cost protein microarray method for detecting serum alpha-fetoprotein (AFP) and AFP-L3 levels. Methods Serum samples from patients with hepatocellular carcinoma (HCC) (n = 33) and control subjects (n = 39) were collected and evaluated for the presence of AFP using a novel protein microarray. Glycoprotein (including AFP-L3) was enriched from crude samples by a Hotgen Biotech glycosyl capture spin column and then detected by protein microarray. An electrochemiluminescence immunoassay (ECLIA) was used to validate the

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25

Di Cristina, Manlio, Luisa Nunziangeli, Maria Angela Giubilei, et al. "An antigen microarray immunoassay for multiplex screening of mouse monoclonal antibodies." Nature Protocols 5, no. 12 (2010): 1932–44. http://dx.doi.org/10.1038/nprot.2010.161.

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26

Xu, Baojian, Qinghui Jin, and Jianlong Zhao. "Multi-layer SU-8 based micro dispensing system for microarray immunoassay." Sensors and Actuators A: Physical 135, no. 1 (2007): 292–99. http://dx.doi.org/10.1016/j.sna.2006.07.003.

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27

Perez-Gordo, Marina, Jing Lin, Ludmilla Bardina, et al. "Epitope Mapping of Atlantic Salmon Major Allergen by Peptide Microarray Immunoassay." International Archives of Allergy and Immunology 157, no. 1 (2012): 31–40. http://dx.doi.org/10.1159/000324677.

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28

Abdullahi, I., and M. Rott. "Microarray immunoassay for the detection of grapevine and tree fruit viruses." Journal of Virological Methods 160, no. 1-2 (2009): 90–100. http://dx.doi.org/10.1016/j.jviromet.2009.04.027.

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29

Hu, Weihua, Xin Li, Guangli He, et al. "Sensitive competitive immunoassay of multiple mycotoxins with non-fouling antigen microarray." Biosensors and Bioelectronics 50 (December 2013): 338–44. http://dx.doi.org/10.1016/j.bios.2013.06.037.

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30

Ruktanonchai, Uracha, Onanong Nuchuchua, Ratthaphol Charlermroj, Thitiporn Pattarakankul, and Nitsara Karoonuthaisiri. "Signal amplification of microarray-based immunoassay by optimization of nanoliposome formulations." Analytical Biochemistry 429, no. 2 (2012): 142–47. http://dx.doi.org/10.1016/j.ab.2012.07.012.

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31

Wang, J., L. Bardina, D. Lencer, W. G. Shreffler, and H. A. Sampson. "Determination of Epitope Diversity in Cow's Milk Hypersensitivity Using Microarray Immunoassay." Journal of Allergy and Clinical Immunology 117, no. 2 (2006): S39. http://dx.doi.org/10.1016/j.jaci.2005.12.161.

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32

Lee, Jonghwan, Okgene Kim, Jaeyeon Jung, Kyunga Na, Pilwoo Heo, and Jinho Hyun. "Simple fabrication of a smart microarray of polystyrene microbeads for immunoassay." Colloids and Surfaces B: Biointerfaces 72, no. 2 (2009): 173–80. http://dx.doi.org/10.1016/j.colsurfb.2009.03.031.

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33

Di, Cristina Manlio, Luisa Nunziangeli, MariaAngela Giubilei, et al. "An antigen microarray immunoassay for multiplex screening of mouse monoclonal antibodies." Nature protocols 5, no. 12 (2010): 1932. https://doi.org/10.1038/nprot.2010.161.

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The mouse monoclonal antibody (mAb) technology still represents a key source of reagents for research and clinical diagnosis, although it is relatively inefficient and expensive and therefore unsuitable for high-throughput production against a vast repertoire of antigens. In this article, we describe a protocol that combines the immunization of individual mice with complex mixtures of influenza virus strains and a microarray-based immunoassay procedure to perform a parallel screening against the viral antigens. The protocol involves testing the supernatants of somatic cell hybrids against a ca

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34

Kuno, Atsushi, Yuzuru Ikehara, Yasuhito Tanaka, et al. "Multilectin Assay for Detecting Fibrosis-Specific Glyco-Alteration by Means of Lectin Microarray." Clinical Chemistry 57, no. 1 (2011): 48–56. http://dx.doi.org/10.1373/clinchem.2010.151340.

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BACKGROUND Despite the progress made in understanding glyco-alterations of specific glycoproteins such as α1-acid glycoprotein (AGP) associated with liver fibrosis, there has been no useful diagnostic assay with a lectin recognizing the fibrosis-specific alteration and an antibody against the core protein. We therefore developed a compatible multiple lectin-antibody sandwich immunoassay on the basis of the results obtained by the lectin microarray analysis for monitoring fibrosis. METHODS AGP-enriched fractions derived from 0.5-μL sera of 125 patients with staging-determined fibrosis (26.4% F0

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Szkola, A., E. M. Linares, S. Worbs, et al. "Rapid and simultaneous detection of ricin, staphylococcal enterotoxin B and saxitoxin by chemiluminescence-based microarray immunoassay." Analyst 139, no. 22 (2014): 5885–92. http://dx.doi.org/10.1039/c4an00345d.

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36

Shlyapnikov, Yuri M., and Elena A. Shlyapnikova. "Ultrasensitive Bead-Based Immunoassay for Real-Time Continuous Sample Flow Analysis." Biosensors 15, no. 5 (2025): 316. https://doi.org/10.3390/bios15050316.

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The performance of heterophase immunoassays is often limited by the kinetics of analyte binding. This problem is partially solved by bead-based assays, which are characterized by rapid diffusion in the particle suspension. However, at low analyte concentrations, the binding rate is still low. Here, we demonstrate a further improvement of analyte binding kinetics in bead-based immunoassays by simultaneously concentrating both an analyte and magnetic beads in a compact spatial region where binding occurs. The analyte is electrophoretically concentrated in a flow cell where beads are magnetically

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Baschirotto, Priscila T., Marco A. Krieger, and Leonardo Foti. "Preliminary multiplex microarray IgG immunoassay for the diagnosis of toxoplasmosis and rubella." Memórias do Instituto Oswaldo Cruz 112, no. 6 (2017): 428–36. http://dx.doi.org/10.1590/0074-02760160509.

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38

Nichkova, Mikaela, Dosi Dosev, Shirley J. Gee, Bruce D. Hammock, and Ian M. Kennedy. "Microarray Immunoassay for Phenoxybenzoic Acid Using Polymer Encapsulated Eu:Gd2O3Nanoparticles as Fluorescent Labels." Analytical Chemistry 77, no. 21 (2005): 6864–73. http://dx.doi.org/10.1021/ac050826p.

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39

Wei, Yu, Gu Ning, Zhang Hai-Qian, Wu Jian-Guo, Wang Yi-Hong, and Klaus-D. Wesche. "Microarray preparation based on oxidation of agarose-gel and subsequent enzyme immunoassay." Sensors and Actuators B: Chemical 98, no. 1 (2004): 83–91. http://dx.doi.org/10.1016/j.snb.2003.09.031.

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Yu, Ling, Yingshuai Liu, Ye Gan, and Chang Ming Li. "High-performance UV-curable epoxy resin-based microarray and microfluidic immunoassay devices." Biosensors and Bioelectronics 24, no. 10 (2009): 2997–3002. http://dx.doi.org/10.1016/j.bios.2009.03.006.

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41

Peltomaa, Riikka, Elena Benito-Peña, Rodrigo Barderas, Ursula Sauer, Martin González Andrade, and María C. Moreno-Bondi. "Microarray-Based Immunoassay with Synthetic Mimotopes for the Detection of Fumonisin B1." Analytical Chemistry 89, no. 11 (2017): 6216–23. http://dx.doi.org/10.1021/acs.analchem.7b01178.

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42

Zhang, Xian, Zuohuan Wang, Yun Fang, et al. "Antibody Microarray Immunoassay for Simultaneous Quantification of Multiple Mycotoxins in Corn Samples." Toxins 10, no. 10 (2018): 415. http://dx.doi.org/10.3390/toxins10100415.

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We developed and tested a prototype of an antibody microarray immunoassay for simultaneous quantitative detection of four typical mycotoxins (aflatoxin B1, ochratoxin A, zearalenone, and fumonisin B1) in corn samples. The test kit consisted of a nitrocellulose membrane layered with immobilized monoclonal antibodies against mycotoxins. During the assay, the mycotoxin-protein conjugates were biotinylated. The signal detection was enhanced by a combination of the biotin-streptavidin system and enhanced chemiluminescence (ECL). This improved the sensitivity of the assay. Under the optimized condit

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43

Li, Nan, Minjie Shen, and Youchun Xu. "A Portable Microfluidic System for Point-of-Care Detection of Multiple Protein Biomarkers." Micromachines 12, no. 4 (2021): 347. http://dx.doi.org/10.3390/mi12040347.

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Protein biomarkers are indicators of many diseases and are commonly used for disease diagnosis and prognosis prediction in the clinic. The urgent need for point-of-care (POC) detection of protein biomarkers has promoted the development of automated and fully sealed immunoassay platforms. In this study, a portable microfluidic system was established for the POC detection of multiple protein biomarkers by combining a protein microarray for a multiplex immunoassay and a microfluidic cassette for reagent storage and liquid manipulation. The entire procedure for the immunoassay was automatically co

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Scorilas, Andreas, Anders Bjartell, Hans Lilja, Christina Moller, and Eleftherios P. Diamandis. "Streptavidin-Polyvinylamine Conjugates Labeled with a Europium Chelate: Applications in Immunoassay, Immunohistochemistry, and Microarrays." Clinical Chemistry 46, no. 9 (2000): 1450–55. http://dx.doi.org/10.1093/clinchem/46.9.1450.

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Abstract Background: The favorable properties of lanthanide chelates compared with conventional fluorescent probes have attracted considerable interest. A Eu3+ chelator, 4,7-bis(chlorosulfophenyl)-1,10-phenanthroline-2,9-dicarboxylic acid (BCPDA), has been synthesized previously. Methods: We here describe immunoassay, immunohistochemistry, and microarray applications of a new streptavidin-based universal polyvinylamine (PVA) detection reagent that is multiply labeled with the europium chelate of BCPDA. Solid-phase time-resolved immunofluorometric assays for biotinylated mouse IgG and prostate-

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Infantino, M., C. Bentow, A. Seaman, et al. "Highlights on Novel Technologies for the Detection of Antibodies to Ro60, Ro52, and SS-B." Clinical and Developmental Immunology 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/978202.

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Objective. We aimed to compare a chemiluminescent immunoassay (CIA, QUANTA Flash) on BIO-FLASH with a multiplex flow immunoassay (MFI) on BioPlex 2200 for the detection of antibodies to Ro60, Ro52, and SS-B.Methods. The study included 241 samples, from patients suffering from systemic autoimmune diseases (n=108) as well as disease controls (n=133). All samples were tested for anti-Ro52, anti-Ro60, and anti-SS-B (La) antibodies on QUANTA Flash (INOVA Diagnostics, San Diego, USA) and BioPlex 2200 (Bio-Rad Laboratories Inc., Hercules, USA). Discrepant samples were tested by two independent method

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46

Hartmann, Michael, Monika Schrenk, Anette Döttinger, et al. "Expanding Assay Dynamics: A Combined Competitive and Direct Assay System for the Quantification of Proteins in Multiplexed Immunoassays." Clinical Chemistry 54, no. 6 (2008): 956–63. http://dx.doi.org/10.1373/clinchem.2007.099812.

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Abstract Background: The concurrent detection and quantification of analytes that vary widely in concentration present a principal problem in multiplexed assay systems. Combining competitive and sandwich immunoassays permits coverage of a wide concentration range, and both highly abundant molecules and analytes present in low concentration can be quantified within the same assay. Methods: The use of different fluorescence readout channels allows the parallel use of a competitive system and a sandwich configuration. The 2 generated assay signals are combined and used to calculate the amount of

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47

Orlov, Alexey V., Juri A. Malkerov, Denis O. Novichikhin, Sergey L. Znoyko, and Petr I. Nikitin. "Multiplex Label-Free Kinetic Characterization of Antibodies for Rapid Sensitive Cardiac Troponin I Detection Based on Functionalized Magnetic Nanotags." International Journal of Molecular Sciences 23, no. 9 (2022): 4474. http://dx.doi.org/10.3390/ijms23094474.

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Express and highly sensitive immunoassays for the quantitative registration of cardiac troponin I (cTnI) are in high demand for early point-of-care differential diagnosis of acute myocardial infarction. The selection of antibodies that feature rapid and tight binding with antigens is crucial for immunoassay rate and sensitivity. A method is presented for the selection of the most promising clones for advanced immunoassays via simultaneous characterization of interaction kinetics of different monoclonal antibodies (mAb) using a direct label-free method of multiplex spectral correlation interfer

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48

Horiuchi, Kurumi Y., Yuan Wang, Scott L. Diamond, and Haiching Ma. "Microarrays for the Functional Analysis of the Chemical-Kinase Interactome." Journal of Biomolecular Screening 11, no. 1 (2005): 48–56. http://dx.doi.org/10.1177/1087057105282097.

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A central challenge in chemical biology is profiling the activity of a large number of chemical structures against hundreds of biological targets, such as kinases. Conventional 32P-incorporation or immunoassay of phosphorylated residues produces high-quality signals formonitoring kinase reactions but is difficult to use in high-throughput screening (HTS) because of cost and the need for well-plate washing. The authors report a method for densely archiving compounds in nanodroplets on peptide or protein substrate-coated microarrays for subsequent profiling by aerosol deposition of kinases. Each

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49

Pomelova, V. G., T. A. Bychenkova, and N. S. Ossin. "PHOSPHAN Microplate Technology-Based Microarray For Detection of IgG Antibodies against West Nile, Crimean Congo Hemorrhagic Fever and Tick-Borne Encephalitis Viruses." Problems of Particularly Dangerous Infections, no. 3(101) (June 20, 2009): 54–58. http://dx.doi.org/10.21055/0370-1069-2009-3(101)-54-58.

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Demonstrated was the possibility to use PHOSPHAN microplate technology to examine human sera and detect simultaneously specific IgG antibodies to three arboviruses, including the West Nile virus (WNV), Crimean Congo Hemorrhagic Fever virus (CCHFV), and Tick-borne encephalitis virus (TBEV). Both sensitivity and specificity of microarray immunoassay approach were similar to those of ELISA tests (when serum specimens were investigated separately). Using the criterion of 2-fold or stronger reaction of the examined serum specimen with homologous antigen than with heterologous one, we succeeded in d

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Jia, Min, Elena Belyavskaya, Patricia Deuster, and Esther M. Sternberg. "Development of a Sensitive Microarray Immunoassay for the Quantitative Analysis of Neuropeptide Y." Analytical Chemistry 84, no. 15 (2012): 6508–14. http://dx.doi.org/10.1021/ac3014548.

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