Analytical Data
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基因名
alaA
- Application
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别名
alaA; yfbQ; b2290; JW2287Glutamate-pyruvate aminotransferase AlaA; EC 2.6.1.2
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种属
Escherichia coli
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0A959
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表达区间
1-405aa
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分子量
61.5 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.












