Anti-Cyp1a2

0.5mg/ml if reconstituted with 0.2ml sterile DI water. CYP1A2 (Cytochrome P450, Subfamily I, Polypeptide 2) is a member of the cytochrome P450 mixed-function oxidase system and is involved in the metabolism of xenobiotics in the body. CYP1A2 is a member of the cytochrome P450 superfamily of enzymes. In humans, the CYP1A2 enzyme is encoded by the CYP1A2 gene. CYP1A2 localizes to the endoplasmic reticulum and its expression is induced by some polycyclic aromatic hydrocarbons (PAHs), some of which are found in cigarette smoke. The CYP1A2 gene encodes a P450 enzyme involved in O-deethylation of phenacetin. Ikeya et al. (1989) found that the human CYP1A2 gene spans almost 7.8 kb and contains 7 exons. The CYP1A2 gene is mapped on 15q24.1. CYP1A2 accounts for nearly 15% of the cytochrome P450 in the human liver. CYP1A2 displays higher activity in men than in women, and is inhibited by oral contraceptives. Inducers of CYP1A2 include cruciferous vegetables. Cigarette smoking has also been shown to increase CYP1A2 activity. Expression of CYP1A2 appears to be induced by various dietary constituents. Protein function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25- hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase- like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation. [The UniProt Consortium]