Analytical Data
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基因名
entH
- Application
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别名
entH;C17orf56;ENTHD2;AP-4 complex accessory subunit Tepsin
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种属
Staphylococcus aureus
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0A0M0
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表达区间
25-241aa
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氨基酸序列
EDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV
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分子量
27.1 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
EntH is a crucial protein in the biosynthesis of enterobactin, a high-affinity iron-chelating siderophore produced by various enteric bacteria, including Escherichia coli. This siderophore plays a significant role in iron acquisition, which is vital for bacterial survival in iron-limited environments, such as those found in the human host. Understanding the function and mechanism of EntH is essential, as it is involved in the modification and maturation of enterobactin, influencing the overall efficiency of iron uptake. The study of EntH can provide insights into bacterial pathogenesis, as iron acquisition is often linked to virulence. Additionally, investigating the structural and functional aspects of EntH may reveal novel targets for antimicrobial drug development, particularly in light of the increasing prevalence of antibiotic-resistant bacteria. Current research focuses on the characterization of EntH through recombinant protein technologies, allowing scientists to study its enzymatic activity, protein-protein interactions, and role in enterobactin biosynthesis in detail. By elucidating the mechanisms by which EntH operates, researchers hope to develop strategies to disrupt its function, thereby limiting bacterial growth and combating infections caused by enteric pathogens. Overall, the study of EntH not only enhances our understanding of microbial physiology but also offers potential avenues for therapeutic intervention in infectious diseases.












