Recombinant Human CD47 Fc Chimera Avi-tag Protein, CF Summary
Accession # Q08722
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human SIRP alpha/CD172a Fc Chimera (Catalog # 4546-SA) is immobilized at 0.1 μg/mL (100 μL/well), Recombinant Human CD47Fc Chimera Avi-tag (Catalog # AVI4670) binds with an ED50 of 6‑48 ng/mL.
2 μg/lane of Recombinant Human CD47 Fc Chimera Avi-tag (Catalog # AVI4670) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 60-70 kDa and 120‑140 kDa, respectively.
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). Human CD47 is an integral membrane protein that consists of a 123 amino acid (aa) extracellular domain (ECD) with a single Ig-like domain, five membrane-spanning regions with short intervening loops, and a 34 aa C-terminal cytoplasmic tail (3). Alternate splicing of human CD47 generates additional isoforms with deletions in the cytoplasmic tail (3). Within the N-terminal ECD, human CD47 shares 63% aa sequence identity with mouse and rat CD47. 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).
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