| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | entA |
| Uniprot No | P0A0L2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-257aa |
| 氨基酸序列 | SEKSEEINEKDLRKKSELQGTALGNLKQIYYYNEKAKTENKESHDQFLQHTILFKGFFTDHSWYNDLLVDFDSKDIVDKYKGKKVDLYGAYYGYQCAGGTPNKTACMYGGVTLHDNNRLTEEKKVPINLWLDGKQNTVPLETVKTNKKNVTVQELDLQARRYLQEKYNLYNSDVFDGKVQRGLIVFHTSTEPSVNYDLFGAQGQYSNTLLRIYRDNKTINSENMHIDIYLYTS |
| 预测分子量 | 31.1 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entA重组蛋白的3篇模拟参考文献示例(注：文献为虚构，仅供格式参考)：
1. **文献名称**: "Heterologous Expression and Functional Analysis of entA in Escherichia coli"
**作者**: Zhang, L. et al.
**摘要**: 本研究报道了从致病性大肠杆菌中克隆entA基因，并在重组系统中表达纯化该蛋白。酶活实验证实entA编码的2.3-二羟基苯甲酸-AMP连接酶在细菌铁载体合成中的关键作用。
2. **文献名称**: "Crystallographic Study of entA Recombinant Protein in Siderophore Biosynthesis"
**作者**: Müller, R. & Schmidt, T.K.
**摘要**: 通过X射线晶体学解析了重组entA蛋白的3D结构，揭示了其底物结合口袋的构象变化，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**: "Kinetic Characterization of Purified entA Enzyme in vitro"
**作者**: Chen, W. et al.
**摘要**: 开发了基于镍柱亲和层析的高效纯化方案，系统分析了重组entA的酶动力学参数(Km=8.2μM，kcat=4.5s⁻¹)，证明其催化效率受镁离子浓度显著调控。
4. **文献名称**: "entA Gene Knockout and Complementation Using Recombinant Protein"
**作者**: Gupta, S. et al.
**摘要**: 构建entA缺陷型菌株后，通过表达重组entA蛋白成功恢复细菌的铁载体分泌能力，荧光定量PCR显示该蛋白可逆向调控铁摄取相关基因表达。
(提示：实际研究中建议通过PubMed或Google Scholar检索真实文献，使用关键词如"entA recombinant protein"+"siderophore"+"expression"进行精确查询)
**Background of entA Recombinant Protein**
The entA recombinant protein is derived from the enterotoxigenic *Escherichia coli* (ETEC), a leading bacterial cause of diarrheal diseases in humans and livestock. ETEC produces heat-stable enterotoxins (STs), with STa (heat-stable toxin A) being a key virulence factor responsible for activating intracellular signaling pathways in host cells, leading to fluid secretion and diarrhea. The entA gene encodes the STa toxin's functional subunit, which binds to guanylyl cyclase C (GC-C) receptors on intestinal epithelial cells, triggering cyclic guanosine monophosphate (cGMP) accumulation and subsequent electrolyte imbalance.
Recombinant entA is engineered through heterologous expression systems, such as *E. coli* or yeast, to produce a purified, biologically active toxin subunit for research and diagnostic applications. Its recombinant form allows for controlled study of STa’s mechanism without handling live pathogens, enhancing safety and reproducibility. Researchers utilize entA to investigate toxin-receptor interactions, develop ETEC vaccines, and design inhibitors targeting STa-mediated pathology.
Additionally, entA serves as a critical component in immunoassays for detecting ETEC infections and evaluating vaccine efficacy. Its structural stability and immunogenicity make it a candidate for subunit vaccines aimed at neutralizing STa activity. Recent advances in protein engineering have further optimized entA’s expression yield and stability, supporting its utility in both basic and translational research. Understanding entA’s role in ETEC pathogenesis continues to inform therapeutic strategies against diarrheal diseases, particularly in resource-limited regions where ETEC infections remain a significant public health burden.
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