FcγRII, also known as CD32, are low affinity IgG Fc receptors. There are three distinct genes encoded (A, B, C) in humans and a single gene in mice. The FcγRII proteins share 89% sequence identity at the amino acid level in their extracellular domains, but their transmembrane and cytoplasmic domains differ significantly. FcγRIIA associates with FcRγ and induces an activating signal upon ligand binding, whereas FcγRIIB associates with FcRγ to induce an inhibitory signal. FcγRIIC is a cross-over between the RIIA and RIIB. ?Its extracellular domain shares 99% sequence identity at amino acid level with FcγRIIB, but the cytoplasmic domain is closely related to FcγRIIA. FcγRIIB, also known as CD32b, consists of an extracellular domain, a transmembrane region and a cytoplasmic tail containing an immunoreceptor tyrosine-based inhibition motif (ITIM). FcγRIIB negatively regulates cell activation, proliferation, endocytosis, phagocytosis, and degranulation. FcγRIIB is expressed on monocytes/macrophages, granulocytes, platelets and mast cells in humans.
Size
100 μg
Concentration
n/a
Applications
BA
Other Names
Low affinity immunoglobulin gamma Fc region receptor II-b, Fc fragment of IgG receptor IIb, IgG Fc receptor II-b, CDw32, Fc-gamma RII-b, FcγRII-b, FcRII-b, CD32b, FCGR2B