Recombinant human Aspartate Aminotransferase protein (His tag)
- Bioactive
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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.
View Alternative Names
cAspAT, Glutamate oxaloacetate transaminase 1, Transaminase A, cCAT, GOT1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human Aspartate Aminotransferase protein (His tag) (AB206809)
15% SDS-PAGE analysis of ab206809 (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
Specifications
Form
Liquid
Additional notes
ab206809 was purified using conventional chromatography techniques.
General info
Function
Biosynthesis of L-glutamate from L-aspartate or L-cysteine (PubMed : 21900944). Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. In addition, catalyzes (2S)-2-aminobutanoate, a by-product in the cysteine biosynthesis pathway (PubMed : 27827456).
Sequence similarities
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Target data
Product promise
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