Affinity
Definition
The binding strength of a single antigen-binding site for one epitope, expressed as the equilibrium dissociation constant (Kd). A lower Kd indicates tighter binding. High-affinity antibodies are preferred in forensic immunoassays because they maintain binding at low antigen concentrations.
Related terms
- Complementarity-determining regions (CDRs)
- Six hypervariable loops, three in the heavy-chain variable domain and three in the light-chain variable domain, that together form the antigen-binding site....
- Cross-reactivity
- The capacity of an antibody raised against one analyte to bind structurally related compounds. In RIA, cross-reactivity is the main driver of...
- Fab fragment
- The antigen-binding fragment of an antibody, consisting of one complete light chain paired with the variable and first constant domain of a...
- Fc region
- The crystallisable fragment of an antibody, formed by the paired constant domains of the two heavy chains. The Fc region mediates effector...
- Monoclonal antibody (mAb)
- An antibody produced by a single hybridoma clone, so that every molecule in the preparation is identical, targets the same epitope, and...
Explained in
- Antibody Structure, Classes, and SpecificityThe binding strength of a single antigen-binding site for one epitope, expressed as the equilibrium dissociation constant (Kd). A lower Kd indicates tighter bi...