SCARB1 / CD36L1 / CLA-1 Protein (His & Fc tag) (recombinant mouse)

Protein Construction: A DNA sequence encoding the mature form of mouse SRB1 (NP_058021.1) extracellular domain (Pro 33-Val 440) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus. Sequence: Pro 33-Val 440. Fusion tag: C-His-Fc Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method. Apparent Molecular Mass: 115-120 kDa. Protein function: Scavenger receptor class B, member 1 (SCARB1), also known as CD36L1, is a member of the scavenger receptor family. SCARB1 is expressed primarily in liver and non placental steroidogenic tissues, and predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane. SCARB1 is proposed as a receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells, and is involved in a wide variety of physilogical processes. As a key component in the reverse cholesterol transport pathway, SCARB1 binds high density lipoproteins (HDLs) and mediates selective cholesterol uptake by a mechanism distinct from the LDL pathway. High density lipoproteins (HDLs) play a critical role in cholesterol metabolism and their plasma concentrations are inversely correlated with risk for atherosclerosis. SCARB1 may thus serve as a useful marker that predicts variation in baseline lipid levels and postprandial lipid response. The mouse SCARB Protein function: Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. Both isoform 1 and isoform 2 act as receptors for HDL, mediating selective uptake of cholesteryl ether and HDL-dependent cholesterol efflux (PubMed:9254074, PubMed:9614139). Also facilitates the flux of free and esterified cholesterol between the cell surface and apoB-containing lipoproteins and modified lipoproteins, although less efficiently than HDL. May be involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity. [The UniProt Consortium]