- 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. Probable receptor for HDL, located in particular region of the plasma membrane, called caveolae. Facilitates the flux of free and esterified cholesterol between the cell surface and extracellular donors and acceptors, such as HDL and to a lesser extent, apoB-containing lipoproteins and modified lipoproteins. Probably involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity. Receptor for hepatitis C virus glycoprotein E2. Binding between SCARB1 and E2 was found to be independent of the genotype of the viral isolate. Plays an important role in the uptake of HDL cholesteryl ester (By similarity).|
|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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