Abcam, ab206809, Recombinant human Aspartate Aminotransferase protein (His tag)

Size: 20µg
Recombinant human Aspartate Aminotransferase protein (His tag) is a Human Full Length protein, in the 1 to 413 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS, Mass Spec.
Key facts
Purity:>95% SDS-PAGE,
Endotoxin level:< 1 EU/µg,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:FuncS, SDS-PAGE, Mass SpecSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Specific activity is > 50 units/mg, and is defined as the amount of enzyme that converts 1umole of a-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25°C.,
Accession:P17174,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.03% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Aspartate Aminotransferase (AST) also known as aspartate transaminase or aspartate transferase is an enzyme important for amino acid metabolism. Mechanically it catalyzes the reversible transfer of an amino group from aspartate to α-ketoglutarate forming oxaloacetate and glutamate. AST has a molecular mass of approximately 92 kDa and is expressed in various tissues with high levels found in liver heart muscle and kidneys. Its presence in these tissues highlights its importance in cellular metabolic processes.
Biological function summary
AST facilitates the interconversion between aspartate and oxaloacetate playing a role in the amino acid and urea cycles. Though not part of a large complex AST works closely with similar enzymes such as alanine aminotransferase (ALT) to maintain amino acid balance and support energy production. This enzymatic activity is important in nitrogen metabolism and glutamate use which are necessary for synthesizing other essential molecules within the cell.
Pathways
AST participates in the citric acid cycle and malate-aspartate shuttle enabling efficient energy production and NADH transport. The enzyme assists in converting oxaloacetate a pivotal intermediate in the citric acid cycle to keep the cycle active ensuring efficient cellular respiration. Additionally in the malate-aspartate shuttle AST works alongside malate dehydrogenase to facilitate the transfer of reducing equivalents across the mitochondrial membrane which is essential for ATP generation.
Elevated AST levels often indicate liver damage such as in hepatitis or cirrhosis reflecting its significant tissue expression. The enzyme is also linked to myocardial infarction as damaged heart muscle releases AST into the bloodstream. In these conditions AST serves as a biomarker for tissue damage often in conjunction with ALT levels allowing clinicians to assess the extent of liver or cardiac injury.