Aspartate aminotransferase (EC 2.6.1.1), Escherichia coli

Aspartate aminotransferase (EC 2.6.1.1) is purified from a recombinant E. coli strain. Aspartate aminotransferase, formerly known as L-glutamic-oxaloacetic transaminase, is a pyridoxal phosphate-dependent enzyme present in hepatocytes and myocytes that catalyses the reversible transfer of an amine group from glutamic acid to oxaloacetic acid, forming alpha-ketoglutaric acid and aspartic acid. It is raised in conditions that affect the heart and liver such as viral hepatitis and myocardial infarction. Following damage to these cells, the enzyme is released into the blood where the level can be measured. The enzyme is provided in 3.2 M ammonium sulphate. Specific activity: 500 U/ml Temperature and pH optimum/stability: The optimum pH and temperature are 8.5 and 25 °C, respectively. Shipping Conditions: Room Temperature. Storage Conditions: 2 °C to 8 °C. Features: >95% pure (SDS-PAGE). aspC, AspAT, b0928, Transaminase A, Aspartate aminotransferase