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  • Home
  • Products
    • KinExA 4000
    • TC1000
    • KinExA 3200 >
      • Autosampler
    • Tube Rotator
    • Trade-Up Program
    • Parts & Accessories
    • Request A Quote
  • KinExA Technology
    • Applications >
      • Affinity & Kinetics
      • Immunoassay
      • Measurement Capabilities >
        • Antibodies
        • Cells
        • Small Molecules
        • Proteins
        • DNA & Aptamers
        • Lipids
        • Viruses & Toxins
        • Serum
        • & More
    • The KinExA Advantage
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    • Request A Presentation
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Cells

"In addition to the simplicity of the approach, the method provides a true measure of the affinity/avidity of the antibody to the native form of cell-surface-expressed targets, including antigens that cannot be produced in soluble forms, and to unknown cell surface antigens.”
Rathanaswami P., Babcook J., Gallo M. 2007. High-affinity binding measurements of antibodies to cell-surface-expressed antigens. Anal Biochem 373: 52-60. http://www.ncbi.nlm.nih.gov/pubmed/17910940

 Cell Publications

  • Rathanaswami P., Babcook J., Gallo M. 2007. High-affinity binding measurements of antibodies to cell-surface-expressed antigens. Anal Biochem 373: 52-60. http://www.ncbi.nlm.nih.gov/pubmed/17910940
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  • Bedinger, D., et al. 2015. Differential pathway coupling of activated insulin receptor drives signaling selectivity by XmetA, an allosteric partial agonist antibody. J Pharmacol Exp Ther 353(1):35-43. http://www.ncbi.nlm.nih.gov/pubmed/25613982​ ​
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  • Xie L., et al. 2005. Measurement of the functional affinity constant of a monoclonal antibody for cell surface receptors using kinetic exclusion fluorescence immunoassay. J Immunol Methods 304: 1-14. http://www.ncbi.nlm.nih.gov/pubmed/16098983

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