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Antigen-antibody Affinity Measurement Service
The non-covalent and reversible antigen-antibody interaction is a combination of hydrogen bonds, hydrophobic interactions, electrostatic and van der Waals forces between an epitope in an antigen and an antibody’s antigen binding site. Kinetic analysis is used to determine the affinity of an antibody to its soluble antigen using surface plasmon resonance (SPR) or biolayer interferometry (BLI), which can measure kon, koff, and kD.
General procedure of antigen-antibody affinity measurement:
A. Antibody is captured on the biacore chip or BLI sensor using an appropriate method.
B. Association and dissociation is measured on the Biacore T100 or the ForteBio Octet QKe using various concentrations of the antigen and the kD is calculated using an appropriate curve-fitting model.
A. Study report of antigen-antibody affinity measurement.