Recombinant Cynomolgus Fc gamma RIII/CD16 Protein, CF Summary
Gly17-Gln208, with a C-terminal 6-His tag
Background: Fc gamma RIII (CD16)
Fc gamma RIII/CD16 is a low/intermediate affinity receptor for polyvalent immune-complexed IgG. It is involved in phagocytosis, secretion of enzymes and inflammatory mediators, antibody-dependent cytotoxicity, and clearance of immune complexes (1-3). Mature cynomolgus Fc gamma RIII consists of a 192 aa ECD with two C2-type
Ig-like domains, a 21 aa transmembrane segment, and a 25 aa cytoplasmic domain (4). In humans, Fc gamma RIIIA/CD16a is expressed as a 50-70 kDa transmembrane activating receptor on NK cells, T cells, monocytes, and macrophages (2). It is closely related to the GPI-linked Fc gamma RIIIB which is expressed on human neutrophils and eosinophils (1, 3). These two proteins share 97% amino acid (aa) identity within their extracellular domains (ECD) (5). Within the ECD, mature cynomolgus Fc gamma RIII shares 92% and 90% aa sequence identity with human Fc gamma RIIIA and Fc gamma RIIIB, respectively. Fc gamma RIII surface expression requires interaction with an accessory chain, either the common gamma -chain or CD3 zeta (8, 9). Glycosylation patterns, electrophoretic mobility, and binding affinity appear to differ between NK cell and monocyte Fc gamma RIIIA (10). Shed forms of both Fc gamma RIIIA and Fc gamma RIIIB can be generated by proteolytic cleavage and retain binding activity (11-14). Shedding from monocytes and macrophages can be triggered by cell activation or phagocytosis (14). Soluble Fc gamma RIII circulates in normal plasma and is elevated in rheumatoid arthritis and in coronary artery diseases (12, 13). Cynomolgus Fc gamma RIII binds to cynomolgus IgG subclasses 1-4, to human IgG1 and 3, and more weakly to human IgG2 and 4 (15).
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