Mouse Anti-CYP1A1 Recombinant Antibody (CBWJC-3533) (V2LY-0125-LY910)

Cytochrome P450 Family 1 Subfamily A Member 1

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997, PubMed:10681376).

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) (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997, PubMed:10681376).

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, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301).

Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation (PubMed:15041462, PubMed:18577768).

Catalyzes the epoxidation of double bonds of certain PUFA (PubMed:15041462, PubMed:19965576, PubMed:20972997).

Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system (PubMed:20972997).

Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer (PubMed:15041462).

May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376).

May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195).

9-cis-retinoic acid biosynthetic process Source: Ensembl
Aging Source: Ensembl
Amine metabolic process Source: Ensembl
Camera-type eye development Source: Ensembl
Cell population proliferation Source: Ensembl
Cellular response to copper ion Source: Ensembl
Cellular response to organic cyclic compound Source: MGI
Coumarin metabolic process Source: Ensembl
Dibenzo-p-dioxin catabolic process Source: Ensembl
Digestive tract development Source: Ensembl
DNA methylation Source: Ensembl
Drug metabolic process Source: BHF-UCL
Epoxygenase P450 pathway Source: Reactome
Estrogen metabolic process Source: UniProtKB
Ethylene metabolic process Source: Reactome
Fatty acid metabolic process Source: UniProtKB
Flavonoid metabolic process Source: Ensembl
Hepatocyte differentiation Source: Ensembl
Hydrogen peroxide biosynthetic process Source: Ensembl
Insecticide metabolic process Source: Ensembl
Lipid hydroxylation Source: BHF-UCL
Long-chain fatty acid biosynthetic process Source: Reactome
Maternal process involved in parturition Source: Ensembl
Omega-hydroxylase P450 pathway Source: Reactome
Porphyrin-containing compound metabolic process Source: Ensembl
Positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
Regulation of metabolic process Source: Reactome
Response to antibiotic Source: Ensembl
Response to arsenic-containing substance Source: Ensembl
Response to drug Source: Ensembl
Response to food Source: Ensembl
Response to herbicide Source: Ensembl
Response to hyperoxia Source: Ensembl
Response to hypoxia Source: Ensembl
Response to immobilization stress Source: Ensembl
Response to iron(III) ion Source: Ensembl
Response to lipopolysaccharide Source: Ensembl
Response to nematode Source: Ensembl
Response to virus Source: Ensembl
Response to vitamin A Source: Ensembl
Response to wounding Source: Ensembl
Retinol metabolic process Source: UniProtKB
Steroid biosynthetic process Source: UniProtKB-KW
Steroid metabolic process Source: BHF-UCL
Vitamin D metabolic process Source: BHF-UCL

Cytoplasm; Endoplasmic reticulum membrane; Microsome membrane; Mitochondrion inner membrane