Cayman Fc?Riiib/Cd16b Hna-1b Allotype (Human, Recombinant); Size-

Low affinity immunoglobulin γ Fc region receptor IIIb (FcγRIIIb) has roles in neutrophil adhesion, phagocytosis, and the respiratory burst.¹ It is encoded by the FCGR3B gene in humans and is comprised of two immunoglobulin-like (Ig-like) extracellular domains that bind to IgG Fc and pentraxins, such as C-reactive protein. FcγRIIIb is synthesized as a precursor with a transmembrane domain and four-residue cytoplasmic domain that are cleaved in the endoplasmic reticulum, following which a glycosylphosphatidylinositol (GPI) anchor is added, which allows for membrane association of the mature protein.^2,1 It can be expressed as three different allotypes known as human neutrophil antigens HNA-1a, HNA-1b, and HNA-1c, which are characterized by differential antibody binding affinities.¹ FcγRIIIb is constitutively expressed in neutrophils and a subset of basophils and is shed from the cell surface as a soluble form via proteolytic cleavage during apoptosis or following neutrophil activation.^1,3 Copy number variation of FCGR3B is associated with an increased risk of systemic lupus erythematosus (SLE) and primary Sjögrens syndrome.⁴ Caymans FcγRIIIb/CD16b HNA-1b allotype (human, recombinant) protein consists of 176 amino acids and has a calculated molecular weight of 20 kDa.

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