Scavenger receptor class B member 1 (SCARB1), also known as SR-BI, is part of the scavenger receptor superfamily, which is composed of many members with diverse structures, expression patterns, and functions. SCARB1 is a multi-ligand cell-surface receptor that mediates the selective uptake of lipid from HDL cholesterol into cells and is expressed in steroidogenic tissues in adult animals. Other ligands of SCARB1 include native, acetylated, or oxidized LDL and anionic phospholipids. SCARB1-deficient mice have elevated HDL levels and increased susceptibility to atherosclerosis on fat feeding, indicating its importance in the regulation of cholesterol homeostasis. Along with CLDN1, LDL-R, and the tetraspanin superfamily member CD81, SCARB1 has been reported to be an entry factor for the Hepatitis C virus. At least two isoforms of SCARB1 are known to exist.
SCARB1 antibody was raised against a 15 amino acid peptide near the amino terminus of human SCARB1.
Anti-SCARB1 antibody produced in rabbit has been used for immunohistochemistry.
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The action of this antibody can be blocked using blocking peptide SBP3500048.
Supplied at approx. 1 mg/mL in phosphate buffered saline containing 0.02% sodium azide.
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