Anti-Cytochrome P450 4F2

Custom conjugation services for this antibody as available (eg. labeling of Anti-Cytochrome P450 4F2 with HRP. Available labels are AF: AF350, AF488, AF555, AF594, AF647, AF680, AF700, AF750. Proteins: HRP, Alkaline Phosphatase, Streptavidin. Tandems: APC, APC/Cy7, APC/AF750, APC/iFluor(TM) 700, APC/iFluor(TM) 750, PE, PE/Cy5, PE/Cy7, PE/AF610, PE/AF700, PE/iFluor(TM) 594, PE/iFluor(TM) 647, PE/iFluor(TM) 700, PE/iFluor(TM) 750, PE/Texas Red(R), PerCP, PerCP/Cy5.5. Small Molecules: Biotin. Traditional Dyes: FITC (Fluorescein), TRITC (Rhodamine), PacBlue, PacOrange, Cy3, Cy5. iFluor: 350, 405, 430, 450, 488, 514, 532, 546, 555, 560, 568, 594, 610, 633, 647, 660, 670, 680, 700, 710, 750, 790, 800, 810, 820, 840, 860, A7. mFluor: UV375, UV460, Violet 450, Violet 500, Violet 510, Violet 540, Blue 570, Green 620, Red 700, Red 780. Protein function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, eicosanoids and vitamins (PubMed:18577768, PubMed:10833273, PubMed:10660572, PubMed:11997390, PubMed:17341693, PubMed:18574070). 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 proinflammatory and anti- inflammatory mediators such as leukotriene B4 (LTB4), lipoxin A4 (LXA4), and several HETEs (PubMed:8026587, PubMed:9799565, PubMed:10833273, PubMed:10660572, PubMed:17341693, PubMed:18574070, PubMed:18577768). 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). [The UniProt Consortium]