Analytical Data
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Gene name
alaC
- Application
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Alternative Names
alaC; yfdZ; b2379; JW2376; Glutamate-pyruvate aminotransferase AlaC; EC 2.6.1.2
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P77434
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Expression Region
1-412aa
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Molecular Weight
62.2 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
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Protein Description
AlaC is a key regulatory protein involved in the biosynthesis of amino acids, particularly in the L-alanine pathway. This protein plays a crucial role in the anabolic and catabolic processes that maintain amino acid homeostasis within cells. Research on AlaC has gained significance due to its potential applications in biotechnology and metabolic engineering. By manipulating the functionality of AlaC, researchers aim to enhance the production of L-alanine and other valuable metabolites in microbial cell factories. Additionally, understanding the structure and function of AlaC can illuminate its role in cellular signaling and metabolic regulation, thereby providing insights into various physiological processes. The elucidation of AlaC's mechanisms may also have broader implications, including the development of novel strategies for bioproduction and the treatment of metabolic disorders. Recent advances in recombinant DNA technology have facilitated the expression and purification of AlaC, allowing for detailed biochemical and structural studies. These investigations are expected to lead to a better understanding of the protein’s dynamics and interactions, ultimately paving the way for innovative approaches to improve amino acid synthesis in industrial applications.
