Fc region
Definition
The crystallisable fragment of an antibody, formed by the paired constant domains of the two heavy chains. The Fc region mediates effector functions including complement activation (IgG, IgM) and binding to Fc receptors on phagocytes, and determines the immunoglobulin class.
Related terms
- Affinity
- The binding strength of a single antigen-binding site for one epitope, expressed as the equilibrium dissociation constant (Kd). A lower Kd indicates...
- 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...
- 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 crystallisable fragment of an antibody, formed by the paired constant domains of the two heavy chains. The Fc region mediates effector functions including...