cytochrome P450 1A1 Antibody (internal region)
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | P04798 |
Other Accession | NP_000490.1, 1543 |
Reactivity | Human |
Host | Goat |
Clonality | Polyclonal |
Concentration | 0.5 mg/ml |
Isotype | IgG |
Calculated MW | 58165 Da |
Gene ID | 1543 |
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Other Names | Cytochrome P450 1A1, 1.14.14.1, CYPIA1, Cytochrome P450 form 6, Cytochrome P450-C, Cytochrome P450-P1, CYP1A1 |
Format | 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | cytochrome P450 1A1 Antibody (internal region) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | CYP1A1 {ECO:0000303|PubMed:10681376, ECO:0000312|HGNC:HGNC:2595} |
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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). |
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
This antibody is not expected to cross-react with the similar P450 1A2
References
Sequence variants at CYP1A1-CYP1A2 and AHR associate with coffee consumption. Sulem P, Gudbjartsson DF, Geller F, Prokopenko I, Feenstra B, Aben KK, Franke B, den Heijer M, Kovacs P, Stumvoll M, Mägi R, Yanek LR, Becker LC, Boyd HA, Stacey SN, Walters GB, Jonasdottir A, Thorleifsson G, Holm H, Gudjonsson SA, Rafnar T, Björnsdottir Hum Mol Genet. 2011 May 15;20(10):2071-7. PMID: 21357676
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