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Background
Receptors that recognize the Fc portion of IgG are divided into three groups designated Fc gamma RI, RII, and RIII, also known respectively as CD64, CD32, and CD16. Fc gamma RI binds IgG with high affinity and functions during early immune responses. Fc gamma RII and RIII are low affinity receptors that recognize IgG as aggregates surrounding multivalent antigens during late immune responses. High affinity immunoglobulin gamma Fc receptor I is also known as FCGR1A, FCG1, FCGR1, CD64 and IGFR1, is a type of integral membrane glycoprotein that binds monomeric IgG-type antibodies with high affinity, which belongs to the immunoglobulin superfamily or FCGR1 family. FCGR1A / CD64 contains 3 Ig-like C2-type (immunoglobulin-like) domains. CD64 is constitutively found on only macrophages and monocytes, but treatment of polymorphonuclear leukocytes with cytokines like IFNγ and G-CSF can induce CD64 expression on these cells.
Source
Recombinant Mouse CD64 protein, His Tag (CD4-M5227) is expressed from human 293 cells (HEK293). It contains AA Glu 25 - Pro 297 (Accession # P26151-1). Predicted N-terminus: Glu 25
Molecular Characterization
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 32.3 kDa. The protein migrates as 40-55 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Endotoxin
Less than 1.0 EU per μg of the Mouse Fc gamma RI, His Tag by the LAL method.
Purity
>95% as determined by SDS-PAGE.
Bioactivity
Please refer to product data sheet.
Formulation
Please refer to data sheet.
Reconstitution
See Certificate of Analysis for details of reconstitution instruction and specific concentration.
Storage
Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C-8°C); After reconstitution under sterile conditions for 1 month (4°C-8°C) or 3 months (-20°C to -70°C).
(1) van Vugt M.J., et al., 1996, Blood 87:3593-3599.
(2) Ernst L.K., et al., 1998, Mol. Immunol. 35:943-954.
(3) van Vugt M.J., 1999, Blood 94:808-817.
(4) Edberg J.C., et al., 1999, J. Biol. Chem. 274:30328-30333.
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