Mouse Fc gamma RIII (CD16) Antibody

Receptors for the Fc region of IgG (Fc gamma Rs) are members of the Ig superfamily that function in the activation or inhibition of immune responses such as degranulation, phagocytosis, ADCC (antibody-dependent cellular toxicity), cytokine release, and B cell proliferation (1‑3). The Fc gamma Rs have been divided into three classes based on close relationships in their extracellular domains; these groups are designated Fc gamma  RI (also known as CD64), Fc gamma  RII (CD32), and Fc gamma  RIII (CD16). Each group may be encoded by multiple genes and exist in different isoforms depending on species and cell type. The CD64 proteins are high affinity receptors (~10^-8‑10^-9 M) capable of binding monomeric IgG, whereas the CD16 and CD32 proteins bind IgG with lower affinities (~10^-6‑10^-7 M) only recognizing IgG aggregates surrounding multivalent antigens (1, 4). Fc gamma Rs that deliver an activating signal either have an intrinsic immunoreceptor tyrosine-based activation motif (ITAM) within their cytoplasmic domains or associate with one of the ITAM-bearing adapter subunits, Fc R gamma or zeta (3, 5). The only inhibitory member in human and mouse, Fc gamma  RIIb, has an intrinsic cytoplasmic immunoreceptor tyrosine-based inhibitory motif (ITIM). The coordinated functioning of activating and inhibitory receptors is necessary for successful initiation, amplification, and termination of immune responses (5). Mouse CD16 is encoded by a single gene. The protein product is a type I transmembrane protein having two extracellular Ig-like domains. It is expressed on a variety of myeloid and lymphoid cells (4) and associates with Fc R gamma to deliver an activating signal upon ligand binding (5). Mouse CD32 is closely related to mouse CD16 throughout its extracellular domain (95% amino acid sequence identity), but has a divergent cytoplasmic domain and functions as an inhibitory receptor. Together these proteins constitute an activating/inhibiting receptor pair to regulate immune responses (5).