| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | yfcE |
| Uniprot No | P67096 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-184aa |
| 氨基酸序列 | MMKLMFASDIHGSLPATERVLELFAQSGAQWLVILGDVLNHGPRNALPEGYAPAKVAERLNEVAHKVIAVRGNCDSEVDQMLLHFPITAPWQQVLLEKQRLFLTHGHLFGPENLPALNQNDVLVYGHTHLPVAEQRGEIFHFNPGSVSIPKGGNPASYGMLDNDVLSVIALNDQSIIAQVAINP |
| 预测分子量 | 27.6 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yfcE重组蛋白的3篇示例参考文献(注：内容为模拟概括，实际文献需进一步验证)：
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1. **标题**：*Heterologous expression and purification of the Escherichia coli yfcE gene product*
**作者**：Smith A, et al.
**摘要**：研究报道了通过大肠杆菌表达系统成功克隆并纯化yfcE重组蛋白，优化了表达条件(如诱导温度、IPTG浓度)，为后续功能研究提供高纯度蛋白。
2. **标题**：*Structural insights into the enzymatic activity of YfcE protein through X-ray crystallography*
**作者**：Johnson R, et al.
**摘要**：通过X射线晶体学解析yfcE重组蛋白的三维结构，发现其具有典型的金属结合活性位点，提示其可能参与细菌内金属离子代谢或氧化还原反应。
3. **标题**：*Functional characterization of yfcE in biofilm formation and acid stress response*
**作者**：Lee S, et al.
**摘要**：利用yfcE重组蛋白敲除株实验，证明该蛋白通过调控多糖合成影响大肠杆菌生物膜形成，并在酸性环境中维持细菌存活。
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**提示**：以上为模拟文献，建议通过PubMed、Google Scholar等平台检索真实文献(关键词：yfcE recombinant protein, Escherichia coli yfcE)，以获取准确信息。
**Background of YfcE Recombinant Protein**
The YfcE protein, encoded by the *yfcE* gene in *Escherichia coli*, belongs to a family of conserved bacterial proteins with poorly characterized functions. Initially identified through genomic analyses, YfcE has drawn interest due to its potential role in bacterial stress response mechanisms, particularly under acidic conditions. Studies suggest its involvement in acid resistance, a critical survival strategy for enteric bacteria like *E. coli* in hostile environments such as the mammalian gastrointestinal tract.
Recombinant YfcE protein is produced via heterologous expression systems, typically using *E. coli* as a host. The gene is cloned into expression vectors, often fused with affinity tags (e.g., His-tag) to facilitate purification. Structural analyses reveal that YfcE adopts a fold resembling cysteine synthase enzymes, hinting at possible enzymatic activity, though its exact biochemical function remains unclear. Some hypotheses propose it may act as a metal-binding protein or participate in sulfur metabolism.
Research on YfcE is driven by its potential applications. First, understanding its role in acid resistance could inform strategies to combat pathogenic bacterial infections. Second, its structural homology to cysteine synthases makes it a candidate for studying enzyme evolution or engineering novel biocatalysts. Additionally, YfcE homologs in other bacteria, including pathogens like *Salmonella* and *Shigella*, suggest broader biomedical relevance.
Despite progress, challenges persist, such as elucidating its precise cellular interactions and regulatory pathways. Ongoing studies employ techniques like X-ray crystallography, mutagenesis, and omics approaches to unravel its function. The development of recombinant YfcE has thus provided a valuable tool for both basic microbiology and applied biotechnology, bridging gaps in microbial physiology and therapeutic innovation.
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