CD16 monoclonal antibody

CD64 (FcgammaRI), CD32 (FcgammaRII), and CD16 (FcgammaRIII) are three classes of the immunoglobulin superfamily. CD64 has a high affinity for IgG with three Ig-like domains while CD32 and CD16 have low affinities with two Ig-like domains. Two genes encode CD16-A and CD16-B resulting only in a 6 amino acid difference in their ectodomains. However, CD16-A has a transmembrane anchor versus CD16-B, which has a glycosylphosphatidylinositol. CD64, CD32, and CD16 are membrane glycoproteins that are expressed by all immunologically active cells and trigger various immune functions (activate B cells, phagocytosis, antibody-dependent cellular cytotoxicity, immune complex clearance, and enhancement of antigen presentation). CD16 cross-linking induces tyrosine phosphorylation (Tyr394) of Lck in NK cells. CD32 has tyrosine-based activation motifs in the cytoplasmic domain in contrast to CD16, which associates with molecules possessing these motifs.