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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ECF |
| Uniprot No | Q9BZP6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-368aa |
| 氨基酸序列 | MVSTPENRQTFITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA |
| 预测分子量 | 67.1kDa |
| 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ECF(假设为细菌胞外功能sigma因子)重组蛋白的3篇示例文献，供参考：
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1. **文献名称**：*Recombinant Production and Purification of the ECF Sigma Factor SigE in Mycobacterium tuberculosis*
**作者**：Rodríguez S, et al.
**摘要**：本研究描述了大肠杆菌中重组表达结核分枝杆菌SigE(ECF sigma因子)的优化策略，通过亲和层析纯化获得高纯度蛋白，并验证其与RNA聚合酶的结合活性，为研究细菌应激反应机制提供工具。
2. **文献名称**：*Engineering ECF Recombinant Proteins for Enhanced Antibiotic Production in Streptomyces*
**作者**：Wang L, et al.
**摘要**：通过重组技术改造链霉菌中的ECF蛋白，显著提高了次级代谢产物(如抗生素)的产量，揭示了ECF因子在调控基因簇表达中的关键作用。
3. **文献名称**：*Structural Insights into ECF Sigma Factor Activation via Recombinant Co-expression Systems*
**作者**：Tanaka K, et al.
**摘要**：利用共表达系统重组制备了ECF sigma因子及其抗σ因子复合物，通过冷冻电镜解析其结构，阐明了环境信号触发的σ因子释放机制。
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**注**：以上文献为示例性内容，实际研究中请根据具体ECF定义(如特定病原体、功能或应用场景)检索权威数据库(PubMed、Web of Science等)。若需精准文献，建议提供ECF的全称或研究背景。
**Background of ECF Recombinant Proteins**
Recombinant proteins derived from the **Extracytoplasmic Function (ECF) σ factors** represent a significant area of research in bacterial stress response and biotechnology. ECF σ factors are a subclass of bacterial sigma proteins that regulate transcription in response to extracellular signals, such as cell envelope stress, oxidative stress, or nutrient limitation. These proteins function by binding to RNA polymerase, directing it to specific promoter regions to initiate the transcription of stress-responsive genes.
The development of recombinant ECF proteins leverages genetic engineering techniques to express and purify these regulatory factors *in vitro*. This enables detailed structural and functional studies, including their interaction with RNA polymerase, DNA-binding specificity, and activation mechanisms. Recombinant ECF proteins are typically produced in heterologous hosts like *Escherichia coli*, using plasmid-based expression systems. Advances in protein purification (e.g., affinity tags) and structural biology (e.g., X-ray crystallography, cryo-EM) have accelerated their characterization.
ECF σ factors are also explored for biotechnological applications. Their ability to sense specific stressors makes them candidates for designing synthetic biological circuits, biosensors, or antimicrobial agents. Additionally, understanding ECF-mediated pathways aids in targeting bacterial stress responses for novel antibiotics. Challenges remain in optimizing recombinant yields, stability, and functional reconstitution *in vivo*. Nonetheless, ECF recombinant proteins continue to bridge fundamental microbiology with applied research, offering insights into bacterial adaptation and tools for synthetic biology.
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