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Recombinant Human CD47 Protein(Fc tag) (HH0207CL)

Recombinant Human CD47 Protein (Q08722) (Met1-Pro139) with the Fc region of human IgG1 at the C-terminus was expressed in HEK293.

Size Price Qty
50ug $429.00
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PRODUCT INFORMATION

Cat.No.
HH0207CL
Synonyms
CD47; IAP; OA3; MER6
Species
Human
Accession
Source
HEK293
Tag
Fc
Predicted N Terminal
Gln 19
Form
Lyophilized from sterile PBS, pH 7.4, 5 % trehalose and 5 % mannitol.
Bio-activity
Measured by its binding ability in a functional ELISA. Immobilized human SIRPA-His at 10 μg/ml (100 μl/well) can bind human CD47-Fc, The EC50 of human CD47-Fc is 10.1-23.5 ng/ml. Measured by its binding ability in a functional ELISA. Immobilized mouse SIRPA-His at 10 μg/ml (100 μl/well) can bind human CD47-Fc, The EC50 of human CD47-Fc is 0.05-0.13 μg/ml. Measured by its binding ability in a functional ELISA. Immobilized human SIRPG-His at 10 μg/ml (100 μl/well) can bind human CD47-Fc, The EC50 of human CD47-Fc is 0.58-1.34 μg/ml.
Molecular Mass
Recombinant Human CD47/Fc is a disulfide-linked homodimer. The reduced monomer comprises 362 amino acids and has a predicted molecular mass of 40.7 kDa. The apparent molecular mass of the protein is approximately 48-60 kDa in SDS-PAGE under reducing conditions.
Endotoxin
< 1.0 EU per 1 microgram of protein (determined by LAL method).
Purity
> 95 % by SDS-PAGE.

BACKGROUND

Background
Has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins. Plays an important role in memory formation and synaptic plasticity in the hippocampus (By similarity). Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. May play a role in membrane transport and/or integrin dependent signal transduction. May prevent premature elimination of red blood cells. May be involved in membrane permeability changes induced following virus infection.
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