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CYP1A1 Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P04798 |
|---|---|
| Clone Names | 80305169 |
| Gene ID | 1543 |
|---|---|
| Other Names | Cytochrome P450 1A1, CYPIA1, Cytochrome P450 form 6, Cytochrome P450-C, Cytochrome P450-P1, CYP1A1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7993c was selected from the C-term region of human CYP1A1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | CYP1A1 {ECO:0000303|PubMed:10681376, ECO:0000312|HGNC:HGNC:2595} |
|---|---|
| Function | 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). |
| Cellular Location | Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Microsome membrane {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00185}. Cytoplasm {ECO:0000250|UniProtKB:P00185} |
| Tissue Location | Lung, lymphocytes and placenta. |
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Provided below are standard protocols that you may find useful for product applications.
Background
CYP1A1 is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein 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 enzyme's endogenous substrate is unknown; however, it is able to metabolize some PAHs to carcinogenic intermediates. CYP1A1 gene has been associated with lung cancer risk.
References
Delpisheh,A., Eur. J. Obstet. Gynecol. Reprod. Biol. 143 (1), 38-42 (2009)Zhuo,W., Cancer Invest. 27 (1), 86-95 (2009)
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