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Cytochrome P450 4F2 Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IP, IHC-P, E |
|---|---|
| Primary Accession | P78329 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 60 KDa |
| Gene ID | 8529 |
|---|---|
| Other Names | Phylloquinone omega-hydroxylase CYP4F2, 20-hydroxyeicosatetraenoic acid synthase, 20-HETE synthase, 11413-, Arachidonic acid omega-hydroxylase, CYPIVF2, Cytochrome P450 4F2, Cytochrome P450-LTB-omega, Leukotriene-B(4) 20-monooxygenase 1, Leukotriene-B(4) omega-hydroxylase 1, CYP4F2 (HGNC:2645) |
| Format | 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50% |
| Storage | Store at -20 °C.Stable for 12 months from date of receipt |
| Name | CYP4F2 {ECO:0000303|PubMed:10492403, ECO:0000312|HGNC:HGNC:2645} |
|---|---|
| Function | A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, eicosanoids and vitamins (PubMed:10660572, PubMed:10833273, PubMed:11997390, PubMed:17341693, PubMed:18574070, PubMed:18577768). 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 (CPR; NADPH-ferrihemoprotein reductase). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of long- and very long-chain fatty acids. Displays high omega-hydroxylase activity toward polyunsaturated fatty acids (PUFAs) (PubMed:18577768). Participates in the conversion of arachidonic acid to omega-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (PubMed:10660572, PubMed:17341693, PubMed:18574070). Plays a role in the oxidative inactivation of eicosanoids, including both pro-inflammatory and anti- inflammatory mediators such as leukotriene B4 (LTB4), lipoxin A4 (LXA4), and several HETEs (PubMed:10660572, PubMed:10833273, PubMed:17341693, PubMed:18574070, PubMed:18577768, PubMed:8026587, PubMed:9799565). Catalyzes omega-hydroxylation of 3-hydroxy fatty acids (PubMed:18065749). Converts monoepoxides of linoleic acid leukotoxin and isoleukotoxin to omega-hydroxylated metabolites (PubMed:15145985). Contributes to the degradation of very long-chain fatty acids (VLCFAs) by catalyzing successive omega-oxidations and chain shortening (PubMed:16547005, PubMed:18182499). Plays an important role in vitamin metabolism by chain shortening. Catalyzes omega-hydroxylation of the phytyl chain of tocopherols (forms of vitamin E), with preference for gamma-tocopherols over alpha-tocopherols, thus promoting retention of alpha-tocopherols in tissues (PubMed:11997390). Omega-hydroxylates and inactivates phylloquinone (vitamin K1), and menaquinone-4 (MK-4, a form of vitamin K2), both acting as cofactors in blood coagulation (PubMed:19297519, PubMed:24138531). |
| Cellular Location | Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein |
| Tissue Location | Liver. Also present in kidney: specifically expressed in the S2 and S3 segments of proximal tubules in cortex and outer medulla (PubMed:10660572). |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
References
Kikuta Y.,et al.FEBS Lett. 348:70-74(1994).
Chen L.,et al.Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
Kikuta Y.,et al.DNA Cell Biol. 18:723-730(1999).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Grimwood J.,et al.Nature 428:529-535(2004).
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