Affinity of an antibody for its target can be measured using either equilibrium or kinetic methods. Equilibrium techniques such as ELISA and FACS measure the EC50 value of the antibody-target binding. Kinetic analyses such as biolayer interferometry (BLI) and surface plasmon resonance (SPR) measure the kon, koff, and KD of the antibody-target interaction.
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1. Antibody is captured on the biacore chip or BLI sensor using an appropriate method.
2. Association and dissociation is measured on the Biacore T100 or the ForteBio Octet QKe using varying concentrations of antigen and the kD is calculated using an appropriate curve-fitting mode.