Anti-CYP4A11 (Aa 229-443) Polyclonal Antibody (DPABH-03690) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use

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Anti-CYP4A11 (aa 229-443) polyclonal antibody (DPABH-03690) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Antigen Description Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate, myristate and palmitate. Has little activity toward prostaglandins A1 and E1. Oxidizes arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE). Immunogen Recombinant fragment, corresponding to a region within amino acids 229-443 of Human Cytochrome P450 4A11/22 (Uniprot ID: Q02928). Isotype IgG Source/Host Rabbit Species Reactivity Human Purification Immunogen affinity purified Conjugate Unconjugated Applications WB, IHC-P, ICC/IF Format Liquid Size 100 μl Buffer pH: 7.00; Constituents: 0.75% Glycine, 1.21% Tris, 20% Glycerol Preservative None Storage Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. GENE INFORMATION Gene Name CYP4A11 cytochrome P450, family 4, subfamily A, polypeptide 12 [ Homo sapiens ] Official Symbol CYP4A11 Synonyms CYP4A11; cytochrome P450, family 4, subfamily A, polypeptide 11; CP4Y; CYP4A2; CYP4AII; cytochrome P450 4A11; CYPIVA11; P450HL-omega; 20-HETE synthase; alkane-1 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved monooxygenase; cytochrome P450HL-omega; cytochrome P-450HK-omega; fatty acid omega- hydroxylase; lauric acid omega-hydroxylase; 20-hydroxyeicosatetraenoic acid synthase; cytochrome P450, subfamily IVA, polypeptide 11; Entrez Gene ID 1579 Protein Refseq NP_000769.2 UniProt ID Q02928 Pathway Arachidonic acid metabolism; Arachidonic acid metabolism; Cytochrome P450 - arranged by substrate type; Fatty Acid Omega Oxidation Function alkane 1-monooxygenase activity; arachidonic acid epoxygenase activity; arachidonic acid omega-hydroxylase activity; heme binding 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved.

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Cytochrome P450 Enzymes in Oxygenation of Prostaglandin Endoperoxides and Arachidonic Acid
Comprehensive Summaries of Uppsala Dissertations from the Faculty of Pharmacy 231 _____________________________ _____________________________ Cytochrome P450 Enzymes in Oxygenation of Prostaglandin Endoperoxides and Arachidonic Acid Cloning, Expression and Catalytic Properties of CYP4F8 and CYP4F21 BY JOHAN BYLUND ACTA UNIVERSITATIS UPSALIENSIS UPPSALA 2000 Dissertation for the Degree of Doctor of Philosophy (Faculty of Pharmacy) in Pharmaceutical Pharmacology presented at Uppsala University in 2000 ABSTRACT Bylund, J. 2000. Cytochrome P450 Enzymes in Oxygenation of Prostaglandin Endoperoxides and Arachidonic Acid: Cloning, Expression and Catalytic Properties of CYP4F8 and CYP4F21. Acta Universitatis Upsaliensis. Comprehensive Summaries of Uppsala Dissertations from Faculty of Pharmacy 231 50 pp. Uppsala. ISBN 91-554-4784-8. Cytochrome P450 (P450 or CYP) is an enzyme system involved in the oxygenation of a wide range of endogenous compounds as well as foreign chemicals and drugs. This thesis describes investigations of P450-catalyzed oxygenation of prostaglandins, linoleic and arachidonic acids. The formation of bisallylic hydroxy metabolites of linoleic and arachidonic acids was studied with human recombinant P450s and with human liver microsomes. Several P450 enzymes catalyzed the formation of bisallylic hydroxy metabolites. Inhibition studies and stereochemical analysis of metabolites suggest that the enzyme CYP1A2 may contribute to the biosynthesis of bisallylic hydroxy fatty acid metabolites in adult human liver microsomes. 19R-Hydroxy-PGE and 20-hydroxy-PGE are major components of human and ovine semen, respectively. They are formed in the seminal vesicles, but the mechanism of their biosynthesis is unknown. Reverse transcription-polymerase chain reaction using degenerate primers for mammalian CYP4 family genes, revealed expression of two novel P450 genes in human and ovine seminal vesicles.
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DMD Fast Forward. Published on July 21, 2011 as DOI: 10.1124/dmd.110.036848 DMD ThisFast article Forward. has not been Published copyedited andon formatted.July 21, The 2011 final asversion doi:10.1124/dmd.110.036848 may differ from this version. DMD #36846 1 Title page CYP4F3B expression is associated with differentiation of HepaRG human hepatocytes and unaffected by fatty acid overload. Stéphanie Madec, Virginie Cerec, Emmanuelle Plée-Gautier, Joseph Antoun, Denise Glaise, Jean-Pierre Salaun, Christiane Guguen-Guillouzo and.Anne Corlu Downloaded from CNRS, UMR 7139, Station Biologique, BP74, 29682 Roscoff Cedex, France. (S.M., J-P. S.) dmd.aspetjournals.org Inserm, UMR–S 991, Liver Metabolisms and Cancer, Université de Rennes 1, CHU Rennes, avenue de la bataille Flandres-Dunkerque, 35033 Rennes, France. (V.C., D.G., C.G-G, A.C.) at ASPET Journals on October 1, 2021 Université de Bretagne Occidentale, Laboratoire de Biochimie, EA-948, Faculté de Médecine, CS 93837, 29238 Brest Cedex 3, France. (E. P-G., J.A., J-P. S) Copyright 2011 by the American Society for Pharmacology and Experimental Therapeutics. DMD Fast Forward. Published on July 21, 2011 as DOI: 10.1124/dmd.110.036848 This article has not been copyedited and formatted. The final version may differ from this version. DMD #36846 2 Running title page Running title: CYP4F3B and ω-hydroxylation of fatty acids in HepaRG cells Corresponding authors: Dr C. Guguen-Guillouzo and Dr A. Corlu, INSERM UMR-S 991, Hôpital Pontchaillou, 35033 Rennes cedex (France), Tel +33 (0)2 23 23 38 52,
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