- CITATIONS: 1
|Reactivity||Human, Mouse, Rat|
|Calculated MW||60878 Da|
|Other Names||Scavenger receptor class B member 1, SRB1, CD36 and LIMPII analogous 1, CLA-1, CD36 antigen-like 1, Collagen type I receptor, thrombospondin receptor-like 1, SR-BI, CD36, SCARB1, CD36L1, CLA1|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human SR-B1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SR-B1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells (PubMed:12016218, PubMed:12519372, PubMed:21226579). Facilitates the flux of free and esterified cholesterol between the cell surface and extracellular donors and acceptors, such as high density lipoproteins (HDL) and to a lesser extent, apoB- containing lipoproteins and modified lipoproteins. Necessary for selective HDL-cholesterol uptake (PubMed:26965621). Probably involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity (PubMed:12016218).|
|Cellular Location||Cell membrane; Multi-pass membrane protein. Membrane, caveola; Multi-pass membrane protein. Note=Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae|
|Tissue Location||Widely expressed.|
Provided below are standard protocols that you may find useful for product applications.
SR-BI is a high density lipoprotein (HDL) receptor. SR-BI binds HDL with high affinity, is expressed primarily in liver and nonplacental steroidogenic tissues, and mediates selective cholesterol uptake by a mechanism distinct from the classic LDL receptor pathway (1). SR-BI mediates the selective uptake of cholesteryl esters from HDL and cholesterol secretion into bile in the liver. CLAMP (C-terminal linking and modulating protein), a four-PDZ-domain-containing protein, is associated with SR-BI in the liver sinusoidal plasma membranes and may modulate the intracellular transport and metabolism of cholesteryl esters taken up from HDL (2). It has also been shown that the hepatitis C virus (HCV) envelope glycoprotein E2 selectively binds to human hepatic cells via SR-BI (3).
1. Acton S, et al. Science 271(5248):518-20, 1996.
2. Ikemoto M, et al. Proc Natl Acad Sci 97(12):6538-43, 2000.
3. Scarselli E, et al. EMBO J, 21(19):5017-25.
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