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形狀
powder
包裝
pkg of 1 × 1 mg (700023P-1mg)
製造商/商標名
Avanti Research™ - A Croda Brand
運輸包裝
dry ice
儲存溫度
−20°C
一般說明
7α,27-dihydroxy-4-cholesten-3-one synthesized by the hydroxylation of 27-hydroxycholesterol in the presence of the enzyme cholesterol 7 α-hydroxylase (CYP7A1) and is catabolized to bile acid. 7α,27-dihydroxy-4-cholesten-3-one is present majorly in fibroblasts and its conversion from cholesterol occurs in extrahepatic tissues.
應用
7α,27-dihydroxy-4-cholesten-3-one may be used as a ligand to test its effect on Epstein-Barr virus-induced molecule 2 (EB12) activation in guanosine 5′-O-(3-thio)triphosphate ([35S] GTPγS) binding assay.
生化/生理作用
7α,27-dihydroxy-4-cholesten-3-one is a suppressor of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase.
包裝
5 mL Amber Glass Screw Cap Vial (700023P-1mg)
法律資訊
Avanti Research is a trademark of Avanti Polar Lipids, LLC
儲存類別代碼
11 - Combustible Solids
Hepatic and extrahepatic dehydrogenation/isomerization of 5-cholestene-3beta, 7alpha-diol: localization of 3beta-hydroxy-Delta5-C27-steroid dehydrogenase in pig tissues and subcellular fractions
Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, 1436(3), 343-353 (1999)
27-Hydroxylated Low Density Lipoprotein (LDL) Cholesterol Can Be Converted to 7alpha, 27-Dihydroxy-4-cholesten-3-one (Cytosterone) before Suppressing Cholesterol Production in Normal Human Fibroblasts EVIDENCE THAT AN ALTERED METABOLISM OF LDL CHOLESTEROL
The Journal of Biological Chemistry, 271(22), 12724-12736 (1996)
Identification of structural motifs critical for epstein-barr virus-induced molecule 2 function and homology modeling of the ligand docking site
Molecular Pharmacology, 82(6), 1094-1103 (2012)
On the substrate specificity of human CYP27A1: implications for bile acid and cholestanol formation.
Journal of lipid research, 44(8), 1515-1522 (2003-06-05)
The mitochondrial sterol 27-hydroxylase (CYP27A1) is required for degradation of the C27-sterol side chain in bile acid biosynthesis. CYP27A1 seems, however, to have roles beyond this, as illustrated by patients with a deficient sterol 27-hydroxylase due to mutations of the
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