Recombinant Mouse SR-BI Fc Chimera Protein, CF Summary
Accession # Q61009-1
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.|
|Reconstitution||Reconstitute at 500 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.
Scavenger Receptor, class B, member 1 (SR-BI), gene name SCARB1, is also known as CD36L1 (CD36-like 1) or CLA-1 (CD36 and LIMPII analogous 1) (1-5). SR-BI is a transmembrane glycoprotein found on macrophages, liver cells and other steroidogenic cells as a lipoprotein receptor. The 509 amino acid (aa) mouse SR-BI contains a central extracellular domain (ECD), flanked by N- and C-terminal transmembrane domains. A mouse splice variant differs at the C-terminal cytoplasmic domain (SR-BII, 506 aa) (2). The mouse SR-BI ECD shares 81% and 92% aa sequence identity with human and rat SR-BI, respectively. SR-BI functions in reverse cholesterol transport (RCT), which is thought to be anti-atherogenic by facilitating transport of cholesteryl esters from macrophages back to the liver for degradation (3). In rodent hepatocytes, SR-BI is the main receptor mediating RCT, while human hepatocytes also express a second mediator, CETP (cholesteryl ester transfer protein) (3-5). On endothelial cells, signaling through SR-BI activates nitric oxide production, which attenuates monocyte adhesion (6). On adrenocortical cells, SR-BI mediates uptake of cholesteryl esters from HDL for the synthesis of glucocorticoid hormones such as cortisol (3-5). On platelets, HDL binding to surface SR-BI inhibits aggregation and increases platelet survival time (3-5). SR-BI and its SR-BII isoform also bind bacterial lipopolysaccharides, facilitating uptake of various bacteria by cells such as peritoneal macrophages (7, 8). This uptake enhances inflammatory responses which, unless properly controlled, can result in sepsis (8-10).
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