Anti-FcgammaRIIb/c Antibody, clone 4F5 clone 4F5, from mouse

FcgammaRI/CD64, FcgammaRII/CD32, FcgammaRIII/CD16, and FcgammaRIV/CD16-2 represent the four known classes of IgG Fc receptors (FcgammaRs). FcgammaRII, FcgammaRIII, and FcgammaRIV are low-affinity receptors for monomeric IgG, whereas FcgammaRI is the only high-affinity FcgammaR. FcgammaRs play important roles in inflammatory cell activation, clearance, presentation of Ag, and maintenance of IgG homeostasis. In addition to binding immune complex (IC), FcgammaRs have been shown to bind non-IgG ligands. For example, FcgammaRII is shown to bind oxLDL, while FcgammaRIII binding to an E. coli component is reported to negatively regulate the function of macrophage receptor with collagenous structure (MARCO). FcyRII activation is also reported to transduce a negative regulatory signal against CD38 crosslinking-induced proliferation of resting mature B cells. Low affinity immunoglobulin gamma Fc region receptor II-a/b/c (IgG Fc receptor II-a/-b/-c, CDw32, Fc-gamma RII-a/-b/-c, Fc-gamma-RIIa/b/c, FcRII-a/-b/-c, CD32) are encoded by the FCGR2A/B/C (CD32, FCG2, IGFR2) genes in human (UniProt P12318, P31994, P31995; Gene ID 2212, 2213, 9103). The FcgammaRIIs encoded by the three genes are highly conserved in their extracellular portion, with significant variation in the transmembrane and intracellular regions. All three types of transcripts alternative splicing to generate additional isoforms.