Recombinant Human CYP1A1 protein
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Recombinant Human CYP1A1 protein is a Human Full Length protein, in the 1 to 512 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
Cytochrome P450 1A1, CYPIA1, Cytochrome P450 form 6, Cytochrome P450-C, Cytochrome P450-P1, Hydroperoxy icosatetraenoate dehydratase, CYP1A1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human CYP1A1 protein (AB114339)
ab114339 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Cytochrome P450 1A1 acts in detoxification processes and is involved in bioactivation of precarcinogens. The enzyme is part of the cytochrome P450 family which consists of many enzymes responsible for metabolizing diverse substrates. CYP1A1's activity can lead to the activation of carcinogens if bioactivated compounds form DNA adducts potentially leading to mutagenesis.
Pathways
CYP1A1 interacts in the aryl hydrocarbon receptor (AhR) signaling pathway and xenobiotic metabolism pathway. In the AhR pathway CYP1A1 participates in the induction of metabolism of environmental pollutants. Within these pathways it works alongside other cytochrome P450 enzymes like CYP1A2 and CYP1B1 both important in similar detoxification processes. The enzyme's regulation affects chemical homeostasis impacting the removal of potential toxins from the body.
Specifications
Form
Liquid
General info
Function
A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed : 10681376, PubMed : 11555828, PubMed : 12865317, PubMed : 14559847, PubMed : 15041462, PubMed : 15805301, PubMed : 18577768, PubMed : 19965576, PubMed : 20972997). 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 : 10681376, PubMed : 11555828, PubMed : 12865317, PubMed : 14559847, PubMed : 15041462, PubMed : 15805301, PubMed : 18577768, PubMed : 19965576, PubMed : 20972997). 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 : 12865317, PubMed : 14559847, 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).
Sequence similarities
Belongs to the cytochrome P450 family.
Subcellular localisation
Mitochondrion inner membrane
Target data
Product promise
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