| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | entG |
| Uniprot No | P0A0L7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-258aa |
| 氨基酸序列 | QPDPKLDELNKVSDYKNNKGTMGNVMNLYTSPPVEGRGVINSRQFLSHDLIFPIEYKSYNEVKTELENTELANNYKDKKVDIFGVPYFYTCIIPKSEPDINQNFGGCCMYGGLTFNSSENERDKLITVQVTIDNRQSLGFTITTNKNMVTIQELDYKARHWLTKEKKLYEFDGSAFESGYIKFTEKNNTSFWFDLFPKKELVPFVPYKFLNIYGDNKVVDSKSIKMEVFLNTH |
| 预测分子量 | 43.0 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entG重组蛋白的3篇文献信息(示例为虚构内容，供参考)：
1. **文献名称**：Cloning and expression of the entG gene encoding a key enzyme in enterobactin biosynthesis
**作者**：Smith A, et al.
**摘要**：本研究克隆了大肠杆菌中的entG基因，通过重组表达纯化得到EntG蛋白，证实其参与肠杆菌素合成的最后修饰步骤，酶活实验表明其催化线性肠杆菌素环化。
2. **文献名称**：Structural characterization of recombinant EntG: Insights into siderophore cyclization
**作者**：Johnson R, et al.
**摘要**：通过X射线晶体学解析了重组EntG蛋白的三维结构，揭示了其底物结合口袋的关键氨基酸残基，为设计针对细菌铁摄取途径的抑制剂提供了结构基础。
3. **文献名称**：Optimization of EntG recombinant protein production in E. coli using tag-free purification
**作者**：Lee S, et al.
**摘要**：开发了无标签的EntG重组蛋白高效纯化工艺，通过温度诱导和离子交换层析获得高纯度蛋白，适用于大规模功能研究及抗菌药物筛选。
(注：以上文献为假设案例，实际研究中请通过PubMed/Google Scholar以关键词"entG recombinant protein"或"enterobactin biosynthesis entG"检索最新文献。)
**Background of entG Recombinant Protein**
The entG gene, derived from *Escherichia coli*, encodes a key enzyme involved in the biosynthesis of enterobactin, a high-affinity iron-chelating siderophore critical for bacterial iron acquisition under iron-limited conditions. Enterobactin enables bacteria to scavenge extracellular iron, essential for growth and virulence, particularly in host environments where iron availability is restricted. The entG product is part of the *ent* operon, which orchestrates the synthesis, modification, and export of enterobactin. Specifically, EntG is proposed to function as a serine hydrolase or esterase, potentially participating in the cyclization or maturation steps of enterobactin assembly, though its precise enzymatic role remains under investigation.
Recombinant entG protein is generated through cloning and heterologous expression in systems like *E. coli* or yeast, followed by purification using affinity chromatography. This engineered protein allows researchers to study its structure, enzymatic activity, and interactions within the enterobactin synthesis pathway. Its recombinant form is particularly valuable for *in vitro* assays, structural analyses (e.g., X-ray crystallography), and inhibitor screening, aiding efforts to disrupt bacterial iron uptake as an antimicrobial strategy.
Interest in entG also stems from its potential applications in biotechnology. Enterobactin-related systems are explored for developing novel antibiotics, biosensors, or iron-delivery systems in agriculture and medicine. Additionally, studying entG provides insights into bacterial adaptation mechanisms and evolutionary strategies for nutrient acquisition. Despite progress, gaps persist in understanding its exact catalytic mechanism and regulatory roles, driving ongoing research to elucidate its contributions to microbial physiology and pathogenicity.
In summary, entG recombinant protein serves as a vital tool for dissecting bacterial iron metabolism and advancing therapeutic innovations against resistant pathogens.
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