Aspartate aminotransferase, Genetically engineered bacteria  (Synonyms: EC 2.6.1.1; GOT; AST)

Aspartate aminotransferase (EC 2.6.1.1), Genetically engineered bacteria is a metabolic regulator with the highest activity in the heart, liver and skeletal muscle. Aspartate aminotransferase, Genetically engineered bacteria comprises two isozymes: the cytoplasmic form (AST1) and the mitochondrial form (AST2). By catalyzing reversible transamination reactions between oxaloacetate, L-glutamate and other substances, it is deeply involved in key physiological processes such as amino acid metabolism, the tricarboxylic acid cycle and neurotransmitter synthesis. Aspartate aminotransferase, Genetically engineered bacteria also provides substrate support for the synthesis of urea and purines/pyrimidines. Aspartate aminotransferase, Genetically engineered bacteria is a serum marker reflecting cardiac and hepatic injury, and its abnormal levels are also closely associated with myocardial infarction, cardiovascular diseases and various cancers^[1][2][3].

Aspartate aminotransferase, Genetically engineered bacteria has increased synthesis and release in adipocytes treated with rosiglitazone (HY-17386), which catalyzes the aminotransferase reaction between aspartate and α-ketoglutarate^[1].

This product can be used as a quality control product for ast kits and as an antigen to prepare anti-cAST antibodies.

Molecular weight: ~58kDa (SDS-PAGE)
pH Stability: 5.0-9.5 (20°C 24 h)
Thermal stability: no deactivation below 60°C for 30 min.
Reconstitution and dilution buffer: It is recommended to use phosphate buffer containing BSA.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9000-97-9

Liquid

Colorless to light yellow

[Aspartate aminotransferase, Genetically engineered bacteria]

2.6.1.1

≥250 U/mL

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Ndrepepa G. Aspartate aminotransferase and cardiovascular disease—a narrative review[J]. Journal of Laboratory and Precision Medicine, 2021, 6.

  [2]. Chambers DA, et al. A longitudinal study of aspartate aminotransferase in human gingival crevicular fluid. J Periodontal Res. 1991;26(2):65-74.

  [3]. Otto-Ślusarczyk D, et al. Aminotransferaza asparaginianowa-kluczowy enzym w metabolizmie ogólnoustrojowym człowieka[J]. Advances in Hygiene & Experimental Medicine/Postepy Higieny i Medycyny Doswiadczalnej, 2016, 70.

  [4]. Ogbuagu E O, et al. Effect of Monosodium glutamate on body weight and alanine aminotransferase activity in wistar rats[J]. International Research Journal of Gastroenterology and Hepatology, 2019, 2(2): 1-8.