Recombinant human CD16 protein was used as the immunogen for the CD16 antibody.
It recognizes CD16 (Fc gamma RIII), the low-affinity receptor for IgG with an apparent molecular weight of 50-80kDa. Two similar genes represent CD16, CD16A (Fc gamma RIIIA), which exists as a hetero-oligomeric polypeptide-anchored form in macrophages and NK cells and CD16B (Fc gamma RIIIB), which exist as a monomeric GPI-anchored form in neutrophils. Furthermore, there are two known polymorphisms of CD16B, NA-1 and NA-2. Individuals homozygous for NA-2 show a lower phagocytic capacity compared with NA-1. CD16 binds IgG in the form of immune complexes and shows preferential binding of IgG1 and IgG3 isotypes and minimal binding of IgG2 and IgG4. Upon IgG binding, both CD16 isoforms initiate signal transduction cascades that lead to a variety of responses including antibody-dependent cell-mediated cytotoxicity (ADCC), phagocytosis, degranulation and proliferation.
