Analytical Data
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Gene name
AST
- Application
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Alternative Names
cCAT; AAT; ASAT; SGOT; GOT1; Cysteine transaminase, cytoplasmic; Transaminase A; Aspartate Transaminase 1,Cytoplasmic; Glutamic-Oxaloacetic Transaminase 1,Soluble
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17174
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Expression Region
Met1~Gln413
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Molecular Weight
44kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of AST (aspartate aminotransferase) recombinant proteins has gained significant attention in the fields of biochemistry and molecular biology due to their pivotal role in amino acid metabolism and the urea cycle. AST is an enzyme that catalyzes the transamination of aspartate and α-ketoglutarate to yield oxaloacetate and glutamate, and it is crucial for cellular energy production and nitrogen metabolism. Research has demonstrated that abnormalities in AST levels are associated with various pathological conditions, including liver disease, myocardial infarction, and metabolic disorders. Recombinant protein technology enables the production of purified AST proteins for in-depth functional studies, enzyme kinetics, and structural analysis. This research is essential for understanding the enzyme's mechanisms, developing diagnostic tools, and exploring potential therapeutic targets. Furthermore, advancements in protein engineering techniques, such as site-directed mutagenesis and expression system optimization, allow for the generation of AST variants with enhanced properties or stability, paving the way for novel applications in biotechnology and medicine. Additionally, the production of recombinant AST proteins can facilitate drug design efforts and the development of biosensors for disease monitoring, highlighting the enzyme's relevance in both clinical and industrial sectors. Overall, the investigation of AST recombinant proteins contributes to a deeper understanding of metabolic pathways and holds promise for future biomedical advancements.











