| 纯度 | >90%SDS-PAGE. |
| 种属 | E. coli |
| 靶点 | cfaE |
| Uniprot No | P25734 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-360aa |
| 氨基酸序列 | MNKILFIFTLFFSSGFFTFAVSADKNPGSENMTNTIGPHDRGGSSPIYNILNSYLTAYNGSHHLYDRMSFLCLSSQNTLNGACPSSDAPGTATIDGETNITLQFTEKRSLIKRELQIKGYKQFLFKNANCPSKLALNSSHFQCNREQASGATLSLYIPAGELNKLPFGGVWNAVLKLNVKRRYDTTYGTYTINITVNLTDKGNIQIWLPQFKSNARVDLNLRPTGGGTYIGRNSVDMCFYDGYSTNSSSLEIRFQDDNSKSDGKFYLKKINDDSKELVYTLSLLLAGKNLTPTNGQALNINTASLETNWNRITAVTMPEISVPVLCWPGRLQLDAKVKNPEAGQYMGNIKITFTPSSQTL |
| 预测分子量 | 41.9 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cfaE重组蛋白的3篇代表性文献(示例格式，具体文献需根据实际研究补充调整)：
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1. **文献名称**：*Structural and functional characterization of the CFA/I adhesin complex of enterotoxigenic Escherichia coli*
**作者**：Mueller, C. et al.
**摘要**：解析了cfaE蛋白与其伴侣蛋白CfaB的复合物晶体结构，揭示了cfaE在介导肠毒素大肠杆菌(ETEC)黏附宿主肠上皮细胞中的关键作用，为靶向黏附机制的疫苗设计提供结构基础。
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2. **文献名称**：*Recombinant cfaE expressed in Escherichia coli as a candidate vaccine antigen against ETEC infections*
**作者**：Li, Y. et al.
**摘要**：构建了重组cfaE蛋白的原核表达系统，证明其能诱导小鼠产生特异性抗体，并在体外实验中显著抑制ETEC菌株的黏附能力，提示其作为疫苗组分的潜力。
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3. **文献名称**：*Immunogenicity and protective efficacy of a cfaE-based subunit vaccine in a murine model*
**作者**：Svennerholm, A. M. et al.
**摘要**：评估了重组cfaE蛋白联合佐剂在动物模型中的免疫效果，结果显示其可诱导黏膜IgA和血清IgG抗体，显著降低ETEC感染后的腹泻发生率。
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4. **文献名称**：*Optimization of recombinant cfaE protein expression and purification for industrial-scale production*
**作者**：Zhang, L. et al.
**摘要**：通过优化表达载体、宿主菌株及纯化工艺，大幅提高了重组cfaE蛋白的产量和稳定性，为大规模疫苗生产提供了技术方案。
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(注：以上文献为示例，实际引用时请核对真实文献信息及数据库收录情况，如PubMed或Google Scholar。)
The cfaE recombinant protein is derived from the CFA/I (Colonization Factor Antigen I) fimbrial adhesin of enterotoxigenic *Escherichia coli* (ETEC), a leading cause of traveler’s diarrhea and pediatric morbidity in low-resource regions. CFA/I fimbriae mediate bacterial adhesion to intestinal epithelial cells, a critical step in ETEC pathogenesis. The cfaE subunit, located at the tip of the fimbria, is responsible for host receptor binding, specifically recognizing glycoconjugates on epithelial surfaces. This interaction facilitates colonization and subsequent toxin delivery, making cfaE a promising target for vaccine development.
Recombinant cfaE is produced through genetic engineering, typically by cloning the *cfaE* gene into expression systems like *E. coli* or yeast. The protein retains key structural features, including its N-terminal receptor-binding domain, which is essential for eliciting neutralizing antibodies. Studies highlight its immunogenicity in animal models, where anti-cfaE antibodies inhibit bacterial adhesion and reduce colonization. This supports its role as a component of subunit vaccines aimed at blocking ETEC infection.
Research on cfaE also addresses challenges such as antigenic variability across ETEC strains and the need for broad protection. Multivalent vaccines combining cfaE with other adhesins (e.g., CS6. LTB) are under investigation. Additionally, structural analyses of cfaE inform epitope-focused designs to enhance immune responses. Despite progress, optimization of expression yield, stability, and scalability remains critical for clinical translation. Overall, cfaE recombinant protein represents a strategic candidate in the effort to combat ETEC-associated diseases through targeted immunological interventions.
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