Analytical Data
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基因名
BFP
- Application
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别名
pBI-SS(Tom)(TP)101-EGFP
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种属
Others
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表达系统
E. coli
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标签
His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
DQ399412
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表达区间
C228-C1455
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蛋白长度
Partial
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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
HtrA (High temperature requirement A) proteins are serine proteases that play crucial roles in bacterial stress response, protein quality control, and pathogenesis. In many pathogenic bacteria, such as *Escherichia coli* and *Helicobacter pylori*, HtrA is involved in the protection of cells under heat shock and other stressful conditions by facilitating the degradation of misfolded proteins. Additionally, it has been implicated in the regulation of virulence factors and can influence biofilm formation, making it an attractive target for antibiotic development. The study of recombinant HtrA proteins has gained momentum, as these proteins can be expressed, purified, and characterized to better understand their structure-function relationships. Recent advances in recombinant DNA technology have enabled researchers to produce large quantities of HtrA proteins, allowing for in-depth biochemical and biophysical analyses. Studying these proteins not only sheds light on their mechanistic roles in bacterial survival and pathogenicity but also opens avenues for therapeutic interventions against bacterial infections. Thus, the exploration of HtrA as a recombinant protein serves as a promising frontier in microbial research and drug development, bridging knowledge gaps that exist in bacterial cell biology and host-pathogen interactions.












