Name : Human Fc gamma RIIIA/CD16a (V176) Domain 2 Protein

Product Source :
Recombinant Human Fc gamma RIIIA/CD16a (V176) Domain 2 Protein is expressed from HEK293 with mFc tag at the C-terminus. It contains Gly107-Thr189.[Accession | AAH17865]

Molecular Weight :
The protein has a predicted MW of 35.29 kDa. Due to glycosylation, the protein migrates to 40-50 kDa based on Tris-Bis PAGE result.

Endotoxin Level :
Less than 1EU per μg by the LAL method.

Purity :
> 95% as determined by Tris-Bis PAGE> 95% as determined by HPLC

Formulation :
Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.

Reconstitution :
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.

Storage and Stability :
-20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3-6 months after reconstitution. 2-8°C for 2-7 days after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.

Product Concentration :
Tris-Bis PAGE Human Fc gamma RIIIA (V176) Domain 2 Protein on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. SEC-HPLC The purity of Human Fc gamma RIIIA (V176) Domain 2 Protein is greater than 95% as determined by SEC-HPLC.

Background :
Human Fc gamma RIIIA/CD16a Protein is a receptor for the Fc region of IgG. Binds complexed or aggregated IgG and also monomeric IgG. Mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis.

Synonyms :
Fc gamma RIIIA; FCGR3; FCGR3A; FCGRIII; FcgRIIIA; FcR-10; CD16A; FCG3; IGFR3; FcRIIIa; FcRIII; CD16; IMD20

References & Citations :
(1)Koene H R , Kleijer M , Algra J , et al. Fc gammaRIIIa-158V/F polymorphism influences the binding of IgG by natural killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-48L/R/H phenotype[J]. Blood, 1997, 90(3):1109-1114.

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