Anti-CYP7A1

0.5mg/ml if reconstituted with 0.2ml sterile DI water. CYP7A1 (Cytochrome P450 Subfamily VIIA Polypeptide 1), also called CYP7, is an enzyme that in humans is encoded by the CYP7A1 gene. Using both mouse-human somatic cell hybrids and in situ chromosomal hybridization, Cohen et al. (1992) mapped the CYP7 gene to 8q11-q12. By transfection of reporter constructs, mutation analysis, and DNase footprinting, Molowa et al. (1992) identified areas of the CYP7A1 promoter region that showed hepatocyte-specific activation. They found HNF3 to be an activator of CYP7A1 activity. Agellon et al. (2002) found that wildtype mice and mice transgenic for human CYP7A1 respond differently to cholesterol feeding. Cholesterol feeding stimulated Cyp7a1 mRNA abundance and enzymatic activity in wildtype mice, but repressed human CYP7A1 mRNA and activity in transgenic mice. Protein function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous cholesterol and its oxygenated derivatives (oxysterols) (PubMed:11013305, PubMed:12077124, PubMed:19965590, PubMed:2384150, PubMed:21813643). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR, NADPH-ferrihemoprotein reductase) (PubMed:2384150, PubMed:11013305, PubMed:12077124, PubMed:19965590, PubMed:21813643). Functions as a critical regulatory enzyme of bile acid biosynthesis and cholesterol homeostasis. Catalyzes the hydroxylation of carbon hydrogen bond at 7-alpha position of cholesterol, a rate-limiting step in cholesterol catabolism and bile acid biosynthesis (PubMed:12077124, PubMed:19965590, PubMed:2384150). 7-alpha hydroxylates several oxysterols, including 4beta-hydroxycholesterol and 24- hydroxycholesterol (PubMed:11013305, PubMed:12077124). Catalyzes the oxidation of the 7,8 double bond of 7-dehydrocholesterol and lathosterol with direct and predominant formation of the 7-keto derivatives (PubMed:21813643). [The UniProt Consortium]