Analytical Data
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基因名
hlyE
- Application
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别名
Cytotoxin ClyA;Hemolysis-inducing protein;Latent pore-forming 34 kDa hemolysin;Silent hemolysin SheA
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种属
Escherichia coli
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表达系统
E. coli
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标签
C- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P77335
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表达区间
2-182aa
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分子量
21.2 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
HlyE, a member of the RTX (Repeats in ToXin) toxin family, is produced by certain pathogenic bacteria, notably within the family of enterobacteria. Research into HlyE has gained significant attention due to its role in bacterial virulence, particularly its ability to form pores in host cell membranes, leading to cell lysis and contributing to tissue damage during infection. Understanding the mechanisms of HlyE, including its structure and interaction with host cells, is crucial for developing strategies to combat infections caused by HlyE-producing pathogens. Recent studies have focused on the recombinant expression of HlyE to produce sufficient quantities for detailed biochemical and structural analysis. This recombinant protein can be used to investigate its functional properties, elucidate its pathogenic mechanisms, and screen for potential inhibitors that might mitigate its harmful effects. Furthermore, the study of HlyE may also contribute to vaccine development or therapeutic interventions against enterobacterial infections. As antibiotic resistance becomes a growing concern in modern medicine, research on HlyE and similar virulence factors is essential for devising new strategies to treat bacterial infections effectively.












