Human CellExp Fc gamma RIIIB /CD16b, human recombinant protein
FCGR3B, CD16B, FCG3B, FCGR3, FCG3, IGFR3
|Calculated MW||This protein is fused with 6×His tag at the C-terminus, has a calculated MW of 21.7 kDa. The predicted N-terminus is Gly 17. DTT-reduced Protein migrates as 38-50 kDa due to glycosylation.|
|Other Names||FCGR3B, CD16B, FCG3B, FCGR3, FCG3, IGFR3|
|Results||Measured by its ability to bind human IgG with an estimated KD < 150 nM.|
|Target/Specificity||Fc gamma RIIIB /CD16b|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.|
|Storage||-20°C; Lyophilized from 0.22 µm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose is added as protectants before lyophilization.|
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Provided below are standard protocols that you may find useful for product applications.
CD16 is a low affinity Fc receptor, and has been identified as Fc receptors FcγRIIIa (CD16a) and FcγRIIIb (CD16b). These receptors bind to the Fc portion of IgG antibodies. CD16 encoded by two different highly homologous genes in a cell type-specific manner. CD16 is found on the surface of natural killer cells, neutrophil polymorphonuclear leukocytes, monocytes and macrophages. CD16B also known as FCGR3B and FCG3B, is expressed specifically by polymorphonuclear leukocytes (neutrophils) and stimulated eosinophils. CD16B is the low affinity receptor for the Fc region of immunoglobulins gamma. FCGR3B binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, FCG3B is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. CD16B may serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils.
Ravetch J.V.,et al.J. Exp. Med. 170:481-497(1989).
Simmons D.,et al.Nature 333:568-570(1988).
Simmons D.,et al.Nature 340:662-662(1989).
Peltz G.A.,et al.Proc. Natl. Acad. Sci. U.S.A. 86:1013-1017(1989).
Scallon B.J.,et al.Proc. Natl. Acad. Sci. U.S.A. 86:5079-5083(1989).
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