Recombinant Mouse CD47 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse SIRP alpha /CD172a Fc Chimera (Catalog # 7154-SA) is coated at 2 μg/mL, Recombinant Mouse CD47 Fc Chimera binds with an apparent Kd <0.6 nM. Also measured by its ability to antagonize mouse red blood cell adhesion to immobilized Recombinant Mouse SIRP alpha /CD172a Fc Chimera (Catalog # 7154-SA). The ED50 for this effect is 2.0-8.0 μg/mL. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived mouse CD47 protein
Gln19 predicted, no results obtained, sequencing might be blocked
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Cd47
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
42.3 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
60-70 kDa, reducing conditions
Publications
Read Publications using 1866-CD in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse CD47 Fc Chimera Protein, CF
antigen identified by monoclonal 1D8
Antigenic surface determinant protein OA3
CD47 antigen (Rh-related antigen, integrin-associated signal transducer)
CD47 antigen
CD47 glycoprotein
CD47 molecule
CD47
IAP
IAPintegrin associated protein
Integrin-associated protein
leukocyte surface antigen CD47
MER6
MER6integrin-associated signal transducer
OA3
Protein MER6
Rh-related antigen
Background
CD47, also known as Integrin‑Associated Protein (IAP) and OA3, is a 40‑60 kDa variably glycosylated atypical member of the immunoglobulin superfamily (1, 2). Mouse CD47 is an integral membrane protein that consists of a 122 amino acid (aa) extracellular domain (ECD) with a single Ig‑like domain, five membrane-spanning regions with short intervening loops, and a 16 aa C‑terminal cytoplasmic tail (3). Alternate splicing of mouse CD47 generates an additional isoform with an insertion of 21 aa following the Ig‑like domain (3). Within the N‑terminal ECD, mouse CD47 shares 63% and 84% aa sequence identity with human and rat CD47, respectively. A portion of the N‑terminal ECD can by shed from smooth muscle cells by MMP-2‑mediated proteolysis (4). The ubiquitously expressed CD47 binds to SIRP family members on macrophages, neutrophils, and T cells (5, 6). These interactions prevent macrophage‑mediated clearance of healthy CD47-expressing cells and promote immune cell transmigration across the vascular endothelium (5‑8). The CD47-SIRP alpha interaction is species specific, and this lack of cross-species interaction has been implicated in xenotransplantation rejection (16). CD47 associates in cis with Fas on T cells and enhances Fas‑mediated apoptosis; its ligation promotes T cell anergy and dampens Th1 immune responses (9‑11). CD47 also associates in cis with Integrins alpha 4 beta 1, alpha V beta 3, alpha 2b beta 3, and alpha 2 beta 1 which can positively or negatively modulate Integrin-mediated function (2, 12). In the vasculature, CD47 binding by Thrombospondin‑1 inhibits the angiogenic and vasorelaxant effects of nitric oxide (2, 13, 14). On dendritic cells and myeloma cells, CD47 ligation by TSP‑1 induces giant cell formation and osteoclast differentiation (15).
Sarfati, M. et al. (2009) Curr. Drug Targ. 9:842.
Isenberg, J.S. et al. (2008) Arterioscler. Thromb. Vasc. Biol. 28:615.
Lindberg, F.P. et al. (1993) J. Cell Biol. 123:485.
Maile, L.A. et al. (2008) Mol. Endocrinol. 22:1226.
Oldenborg, P.-A. et al. (2000) Science 288:2051.
Liu, Y. et al. (2002) J. Biol. Chem. 277:10028.
Stefanidakis, M. et al. (2008) Blood 112:1280.
de Vries, H.E. et al. (2002) J. Immunol. 168:5832.
Manna, P.P. et al. (2005) J. Biol. Chem. 280:29637.
Avice, M.-N. et al. (2001) J. Immunol. 167:2459.
Bouguermouh, S. et al. (2008) J. Immunol. 180:8073.
Barazi, H.O. et al. (2002) J. Biol. Chem. 277:42859.
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