Analytical Data
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Gene name
alaA
- Application
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Alternative Names
alaA; yfbQ; b2290; JW2287Glutamate-pyruvate aminotransferase AlaA; 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
P0A959
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Expression Region
1-405aa
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Molecular Weight
61.5 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
AlaA, a notable amino acid racemase, plays a critical role in the biosynthesis of amino acids, particularly in bacteria and certain fungi. Its primary function is to catalyze the interconversion between L-alanine and D-alanine, the latter being a vital component in bacterial cell wall synthesis. Understanding the mechanisms of AlaA is essential not only for elucidating fundamental biological processes but also for its implications in antibiotic resistance and the development of new antimicrobial agents. The demand for effective treatments against resistant bacterial strains has prompted researchers to investigate the biochemical pathways and structural characteristics of AlaA. In recent years, recombinant protein technology has been leveraged to produce AlaA in a controlled lab environment, enabling detailed studies on its enzymatic activity, substrate specificity, and potential inhibitors. Additionally, the recombinant protein can be utilized for high-throughput screening of compounds that may disrupt its function, presenting a promising avenue for therapeutic interventions. This research not only enhances our understanding of aminotransferases but also opens new doors for drug discovery aimed at combating bacterial infections, which are a growing public health concern. The work around AlaA and its recombinant proteins holds significant promise for advancing both basic science and practical applications in the field of microbiology and pharmaceuticals.
