| 纯度 | >90%SDS-PAGE. |
| 种属 | Staphylococcus aureus |
| 靶点 | entH |
| Uniprot No | P0A0M0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-241aa |
| 氨基酸序列 | EDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV |
| 预测分子量 | 27.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于entH重组蛋白的3篇参考文献示例，涵盖功能、结构及应用研究：
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1. **文献名称**：*Functional Characterization of the entH Gene Product in Escherichia coli Iron Acquisition*
**作者**：Smith, J.R., et al.
**摘要**：本研究成功在大肠杆菌中克隆并表达了重组EntH蛋白，证实其参与肠杆菌素的结合与铁摄取途径。通过体外实验发现，EntH缺失株的铁吸收效率显著降低，提示其在细菌铁载体系统中的关键作用。
2. **文献名称**：*Crystal Structure and Biochemical Analysis of EntH: A Key Enzyme in Enterobactin Biosynthesis*
**作者**：Lee, S., & Kim, H.
**摘要**：作者解析了EntH重组蛋白的X射线晶体结构(分辨率2.1Å)，揭示其独特的结构域排列及活性位点特征。生化实验进一步证明EntH在肠杆菌素合成中催化酯键形成，为抗菌靶点设计提供依据。
3. **文献名称**：*Recombinant EntH as a Novel Vaccine Candidate Against Escherichia coli Infections*
**作者**：Johnson, M.T., et al.
**摘要**：研究评估了重组EntH蛋白的免疫保护效果。动物实验显示，接种EntH的小鼠对致病性大肠杆菌攻击的存活率显著提高，表明其作为疫苗组分的潜在应用价值。
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注：上述文献为模拟示例，实际引用需根据具体研究核实。如需扩展检索，建议结合关键词“entH recombinant protein”、“iron acquisition”、“Escherichia coli”在PubMed或Web of Science等平台查询。
EntH is a bacteriocin-associated protein encoded by the *entH* gene, primarily identified in certain *Enterococcus* species, notably *Enterococcus faecium*. Bacteriocins are antimicrobial peptides produced by bacteria to inhibit competing microbial strains, offering ecological advantages in niche environments. EntH is part of the entHD gene cluster, which is involved in the biosynthesis and secretion of the bacteriocin enterocin H, a ribosomally synthesized and post-translationally modified peptide (RiPP). Enterocin H exhibits broad-spectrum antimicrobial activity against Gram-positive bacteria, including foodborne pathogens like *Listeria monocytogenes* and *Staphylococcus aureus*, making it a candidate for food preservation and therapeutic applications.
Recombinant EntH protein is generated through heterologous expression systems, typically using *Escherichia coli* or *Lactococcus lactis* as hosts. The gene encoding EntH is cloned into expression vectors, allowing controlled production and purification. Structural studies suggest EntH functions as an immunity protein, protecting the producer strain from self-inhibition by neutralizing the bacteriocin’s activity. This mechanism involves specific interactions between EntH and the bacteriocin, preventing pore formation or enzymatic degradation of the producer cell’s membrane.
Research on EntH highlights its potential in biotechnological and medical contexts, particularly in developing novel antimicrobial agents amid rising antibiotic resistance. However, challenges remain in optimizing expression yields, stability, and delivery systems for large-scale applications. Further exploration of EntH’s molecular interactions and regulatory pathways could enhance its utility in both food safety and clinical settings, aligning with global efforts to combat pathogenic threats sustainably.
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