Anti-Lanosterol 14-alpha demethylase / CYP51A1

0.5mg/ml if reconstituted with 0.2ml sterile DI water. P450 enzymes constitute a family of monooxygenase enzymes that are involved in the metabolism of a wide array of endogenous and xenobiotic compounds. Several P450 enzymes have been classified by sequence similarities as members of the CYP1A and CYP2A subfamilies. CYP51A1 (cytochrome P450, family 51, subfamily A, polypeptide 1), also known as LDM (lanosterol 14-alpha demethylase) or cytochrome P450-14DM, is a 503 amino acid protein localized to endoplasmic reticulum membrane. CYP51A1 is an important enzyme for zymosterol and steroid biosynthesis. CYP51A1 catalyzes C14-demethylation of lanosterol, transforming lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. CYP51A1 is ubiquitously expressed, with highest levels found in liver, ovary, testis, lung, kidney and prostate. Protein function: A cytochrome P450 monooxygenase involved in sterol biosynthesis. Catalyzes 14-alpha demethylation of lanosterol and 24,25- dihydrolanosterol likely through sequential oxidative conversion of 14- alpha methyl group to hydroxymethyl, then to carboxylaldehyde, followed by the formation of the delta 14,15 double bond in the sterol core and concomitant release of formic acid (PubMed:20149798, PubMed:8619637). 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:20149798, PubMed:8619637). [The UniProt Consortium]