Fc-γRIII (CD16) is a low affinity receptor involved in interactions with immune complexes. It is a 50 – 80 kDa protein with two distinct forms encoded by two different genes: IIIA and IIIB. The transmembrane form (Fc-γRIIIA) is expressed on NK cells, monocytes and macrophages. The IIIB mRNA encodes FcγRIIIB, a glycoprotein anchored to the outer leaflet of the membrane by a glycosylphosphatidyl-inositol (GPI) moiety and is transcribed only in human neutrophils. FcγRIIIB (CD16b) may act with FcγRIIA (CD32) expressed on neutrophils to mediate antibody-dependent cytotoxicity (ADCC) and phagocytocis. The GPI-linked receptor exists in a soluble form (sCD16) revealing an immunoregulatory function through interaction with complement receptors.
|Clone: 1D3||Isotype: IgM Mouse|
|The monoclonal antibody 1D3 was shown to be non-reactive with NK cells or monocytes but to be specific to polymorphonuclear leucocytes (PMNs). It recognizes an epitope specific to the FcγRIIIB molecule and was characterized as the sole antibody belonging to the CD16b cluster of differentiation. This antibody reacts with PMNs, irrespective of the neutrophil antigen (NA) phenotype, although it shows lower reactivity with NA2- homozygote PMNs as compared to NA1-homozygotes or NA1/NA2 heterozygotes.
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