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 (Probable).

Cytochrome P450 1A2;CP12; P3-450; P450(PA)

p05177

Human

WB,IHC,IF,ICC,FC

WB 1:2000
IHC 1:50
IF 1:100
ICC 1:100-1:400
FC 1:100

Monoclonal

58.2 kDa

Mouse

Full length human recombinant protein of human CYP1A2 (NP_000752) produced in HEK293T cell.

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.