Fc gamma RIIB/CD32b Protein, Cynomolgus (Biotinylated, HEK293, His-Avi)

Fc γ RIIB/CD32b proteins exhibit low affinity as complexes or receptors that aggregate the immunoglobulin γFc region. ITIM phosphorylated by Fc γ RIIB/CD32b recruits inositol phosphatases SHIP1 and SHIP2, inhibits Ras activation, down-regulates MAPK activity, reduces PLC-γ function, and results in PKC activation. Inhibition of MAP kinase pathway and anti-apoptotic kinase Akt inhibit cell proliferation and survival. Fc gamma RIIB/CD32b Protein, Cynomolgus (Biotinylated, HEK293, His-Avi) is the recombinant cynomolgus-derived Fc gamma RIIB/CD32b protein, expressed by HEK293 , with C-Avi, C-His labeled tag.

Fc γ RIIB/CD32b proteins exhibit low affinity as complexes or receptors that aggregate the immunoglobulin γFc region. It plays a key role in a variety of effects and regulatory functions, including phagocytosis of immune complexes and regulation of B-cell antibody production. Upon binding to this receptor, down-regulation of the previous state of cell activation is triggered by an antigen receptor on B cells (BCR), T cells (TCR), or another Fc receptor. The IIB1 subtype does not mediate endocytosis or phagocytosis, while the IIB2 subtype does not induce phagocytosis. Fc γ RIIB/CD32b interacts with INPP5D/SHIP1, FGR, and LYN. Fc γ RIIB/CD32b -phosphorylated ITIM recruits inositol phosphatases SHIP1 and SHIP2, inhibits Ras activation, down-regulates MAPK activity, reduces PLC-γ function, and results in PKC activation. Inhibition of MAP kinase pathway and anti-apoptotic kinase Akt inhibit cell proliferation and survival^[1][2][3].

Cynomolgus

HEK293

C-Avi;C-His

Q8SPW3 (A45-G220)

102139530  [NCBI]

Partial

Biotin

AAPPKAVLKLEPPWINVLREDSVTLTCGGAHSPDSDSTQWFHNGNLIPTHTQPSYRFKANNNDSGEYRCQTGRTSLSDPVHLTVLSEWLALQTPHLEFREGETILLRCHSWKDKPLIKVTFFQNGISKKFSHMNPNFSIPQANHSHSGDYHCTGNIGYTPYSSKPVTITVQVPSMG

Approximately 34 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.