SR-BI/SCARB1 Protein, Human (HEK293, His-Fc)

The SR-BI/SCARB1 protein is a multifunctional receptor that binds a variety of ligands, including phospholipids, cholesteryl esters, lipoproteins, phosphatidylserine, and apoptotic cells. As an HDL receptor, it crucially mediates selective cholesterol ether uptake and HDL-dependent cholesterol efflux. SR-BI/SCARB1 Protein, Human (HEK293, His-Fc) is the recombinant human-derived SR-BI/SCARB1 protein, expressed by HEK293 , with C-hFc, C-His labeled tag.

SR-BI/SCARB1 Protein, functioning as a versatile receptor, binds to various ligands, including phospholipids, cholesterol ester, lipoproteins, phosphatidylserine, and apoptotic cells. As a receptor for HDL, it plays a crucial role in the selective uptake of cholesteryl ether and HDL-dependent cholesterol efflux. Additionally, SR-BI facilitates the exchange of free and esterified cholesterol between the cell surface and apoB-containing lipoproteins, albeit less efficiently than with HDL. Its involvement in phagocytosis of apoptotic cells, mediated by its phosphatidylserine binding activity, adds another layer to its functional repertoire. In the context of microbial infection, SR-BI acts as a receptor for the hepatitis C virus in hepatocytes, facilitating its cellular entry independently of the viral isolate genotype. The diverse ligand interactions and roles in cholesterol homeostasis, apoptotic cell clearance, and viral infection highlight SR-BI/SCARB1 as a multifunctional player in cellular processes.

Human

HEK293

C-hFc;C-His

Q8WTV0-1/NP_001076428.1 (P33-Y443)

949  [NCBI]

PSLIKQQVLKNVRIDPSSLSFNMWKEIPIPFYLSVYFFDVMNPSEILKGEKPQVRERGPYVYREFRHKSNITFNNNDTVSFLEYRTFQFQPSKSHGSESDYIVMPNILVLGAAVMMENKPMTLKLIMTLAFTTLGERAFMNRTVGEIMWGYKDPLVNLINKYFPGMFPFKDKFGLFAELNNSDSGLFTVFTGVQNISRIHLVDKWNGLSKVDFWHSDQCNMINGTSGQMWPPFMTPESSLEFYSPEACRSMKLMYKESGVFEGIPTYRFVAPKTLFANGSIYPPNEGFCPCLESGIQNVSTCRFSAPLFLSHPHFLNADPVLAEAVTGLHPNQEAHSLFLDIHPVTGIPMNCSVKLQLSLYMKSVAGIGQTGKIEPVVLPLLWFAESGAMEGETLHTFYTQLVLMPKVMHY

Approximately 100-120 kDa due to the glycosylation.

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.