Analytical Data
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Gene name
AST
- Application
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Alternative Names
AST；Sialin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
1-413aa
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AA Sequence
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKIANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAIRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPAQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
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Molecular Weight
48 kDa
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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
AST (aspartate aminotransferase) is a vital enzyme involved in amino acid metabolism, playing a crucial role in the transamination process, which helps in the synthesis and degradation of amino acids. Research into recombinant AST proteins has gained momentum due to their potential applications in biotechnology and medicine. Recombinant DNA technology enables the expression of AST in various host systems, allowing for the production of large quantities of the enzyme for analytical and therapeutic purposes. The ability to produce AST in a controlled environment facilitates detailed studies on its structure-function relationships, enzyme kinetics, and interactions with other biomolecules. Furthermore, engineered AST variants with enhanced stability or altered substrate specificity can lead to innovative solutions in drug development and metabolic engineering. Understanding AST mechanisms can also provide insights into metabolic disorders and facilitate the identification of novel biomarkers for clinical diagnostics. Overall, the study of recombinant AST proteins underscores the intersection of molecular biology and applied sciences, aiming to harness the enzyme's properties for advancing biotechnological applications and therapeutic strategies.
