Aspartate Aminotransferase (AST, GOT), Human Liver

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BioVision 05/18 For research use only Aspartate Aminotransferase (AST, GOT), Human Liver CATALOG NO: P1299-100 1 units RELATED PRODUCTS: ALTERNATE NAMES: Aspartate Transaminase, Glutamate Oxaloacetate, AST, GOT, Aspartate Aminotransferase (AST) (Mouse) ELISA Kit (Cat. No. E4320) sGOT, AspAT, ASAT, serum glutamic oxaloacetic transaminase, AAT Aspartate Aminotransferase (AST) (Human) ELISA Kit (Cat. No. E4319) Aspartate Aminotransferase (AST) (Rat) ELISA Kit (Cat. No. E4321) SOURCE: Human Liver Aspartate Aminotransferase (AST or SGOT) Activity Colorimetric Assay Kit (Cat. PURITY: Purified No. K753) Anti-GOT2 Antibody (cat. No. A1273) MOL. WEIGHT: ~92 kDa Anti-GOT1 Antibody (Cat. No. A1272) FORM: Lyophilized GOT2, human recombinant (Cat. No. 7809) GOT1, human recombinant (Cat. No. 7808) STORAGE CONDITIONS: Store at -20°C. Avoid repeated freezing and thawing cycles. BIOLOGICAL ACTIVITY: ≥ 1 U/mg (Dimension® Clinical Chemistry System) UNIT DEFINITATION: One unit will catalyze the transamination of one micromole of L- aspartate to alpha-ketoglutarate forming L-glutamate and oxaloacetate per minute at 37°C and pH 7.8.Measured at 340 nm as one equimolar amount of NAD produced by a coupled reaction. RECONSTITUTION: > 1 mg/mL in tris buffered saline, 1% BSA, pH 8.0. AST/SGOT is found in many tissues throughout the body, including DESCRIPTION: the liver, heart, muscles, kidney, and brain. If any of these organs or tissues is affected by disease or injury, AST is released into the bloodstream. This means that AST isn't as specific an indicator of liver damage as ALT (also known as alanine aminotransferase, another type of enzyme found almost entirely in the liver). The ratio of AST and ALT levels are commonly used as biomarkers for liver health. FOR RESEARCH USE ONLY! Not to be used on humans. BioVision Incorporated Tel: 408-493-1800 | Fax: 408-493-1801 155 S. Milpitas Boulevard, Milpitas, CA 95035 USA www.biovision.com | [email protected] .

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Ornithine Aminotransferase, an Important Glutamate-Metabolizing Enzyme at the Crossroads of Multiple Metabolic Pathways
biology Review Ornithine Aminotransferase, an Important Glutamate-Metabolizing Enzyme at the Crossroads of Multiple Metabolic Pathways Antonin Ginguay 1,2, Luc Cynober 1,2,*, Emmanuel Curis 3,4,5,6 and Ioannis Nicolis 3,7 1 Clinical Chemistry, Cochin Hospital, GH HUPC, AP-HP, 75014 Paris, France; [email protected] 2 Laboratory of Biological Nutrition, EA 4466 PRETRAM, Faculté de Pharmacie, Université Paris Descartes, 75006 Paris, France 3 Laboratoire de biomathématiques, plateau iB2, Faculté de Pharmacie, Université Paris Descartes, 75006 Paris, France; [email protected] (E.C.); [email protected] (I.N.) 4 UMR 1144, INSERM, Université Paris Descartes, 75006 Paris, France 5 UMR 1144, Université Paris Descartes, 75006 Paris, France 6 Service de biostatistiques et d’informatique médicales, hôpital Saint-Louis, Assistance publique-hôpitaux de Paris, 75010 Paris, France 7 EA 4064 “Épidémiologie environnementale: Impact sanitaire des pollutions”, Faculté de Pharmacie, Université Paris Descartes, 75006 Paris, France * Correspondence: [email protected]; Tel.: +33-158-411-599 Academic Editors: Arthur J.L. Cooper and Thomas M. Jeitner Received: 26 October 2016; Accepted: 24 February 2017; Published: 6 March 2017 Abstract: Ornithine δ-aminotransferase (OAT, E.C. 2.6.1.13) catalyzes the transfer of the δ-amino group from ornithine (Orn) to α-ketoglutarate (aKG), yielding glutamate-5-semialdehyde and glutamate (Glu), and vice versa. In mammals, OAT is a mitochondrial enzyme, mainly located in the liver, intestine, brain, and kidney. In general, OAT serves to form glutamate from ornithine, with the notable exception of the intestine, where citrulline (Cit) or arginine (Arg) are end products.
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Supplementary Materials
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Supporting Information
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Supplementary Table 2
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