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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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Antibodies


"By tailoring the KinExA to each studied antigen, we obtained apparent equilibrium dissociation constants (K(D) values) spanning six orders of magnitude, from approximately 100 fM to 100 nM."
Bee C. et. al. 2012. Exploring the dynamic range of the kinetic exclusion assay in characterizing antigen-antibody interactions. PLOS ONE. 7(4). http://www.ncbi.nlm.nih.gov/pubmed/22558410.

 Antibody References

  • Fan Y., et al. 2016. Immunological Characterization and Neutralizing Ability of Monoclonal Antibodies Directed Against Botulinum Neurotoxin Type H. The Journal of Infectious Diseases 15;213(10):1606-14. https://www.ncbi.nlm.nih.gov/pubmed/26936913

  • Köck, K., et al. 2015. Preclinical development of AMG 139, a human antibody specifically targeting IL-23. British Journal of Pharmacology 172:159-172. http://www.ncbi.nlm.nih.gov/pubmed/25205227
​
  • Bee C. et. al. 2012. Exploring the dynamic range of the kinetic exclusion assay in characterizing antigen-antibody interactions. PLOS ONE. 7(4). http://www.ncbi.nlm.nih.gov/pubmed/22558410.
​​
  • Tabrizi M.A., et al. 2009. Translational strategies for development of monoclonal antibodies from discovery to the clinic. Drug Discov Today 14(5/6): 298-305. http://www.ncbi.nlm.nih.gov/pubmed/19152840

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