纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | F17a-A |
Uniprot No | P11312 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 22-180aa |
氨基酸序列 | YDGKITFNGKVVDQTCSVTTESKNLTVKLPTVSANSLASSGKVVGLTPFTILLEGCNTPAVTGAQNVNAYFEPNANTDYTTGNLTNTASSGASNVQIQLLNADGVKAIKLGQAAAAQSVDTVAINDANVTLRYNAQYYATGVATAGDVTSTVNYTIAYQ |
预测分子量 | 32.4 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F17a-A重组蛋白的3篇参考文献示例(内容为模拟虚构,仅供参考):
1. **文献名称**:Molecular characterization of F17a-A adhesin in Escherichia coli isolates from calves
**作者**:Lintermans, P.F., et al.
**摘要**:该研究通过基因克隆和表达技术获得重组F17a-A蛋白,证实其在介导大肠杆菌对牛肠道上皮细胞粘附中的关键作用,为疫苗开发提供靶点。
2. **文献名称**:Recombinant F17a-A production and its immunogenicity in a murine model
**作者**:Bertschinger, H.U., et al.
**摘要**:报道了F17a-A重组蛋白在哺乳动物细胞中的高效表达,动物实验显示其可诱导特异性抗体反应,提示其作为抗腹泻疫苗组分的潜力。
3. **文献名称**:Structural analysis of F17a-A fimbrial subunit using X-ray crystallography
**作者**:Chandran, V., et al.
**摘要**:解析了重组F17a-A蛋白的三维结构,揭示了其受体结合域的保守性特征,为基于结构的抑制剂设计奠定基础。
注:以上文献信息为示例,实际研究中请通过PubMed或Google Scholar以“F17a-A recombinant protein”“F17 fimbriae”等关键词检索真实文献。
**Background of F17a-A Recombinant Protein**
F17a-A is a recombinant protein derived from the F17 fimbrial subunit of *Escherichia coli* (E. coli), a Gram-negative bacterium commonly associated with gastrointestinal infections in humans and animals. F17 fimbriae are filamentous adhesive structures expressed by pathogenic E. coli strains, particularly those infecting the intestinal tract of calves, lambs, and humans. These fimbriae mediate bacterial attachment to host epithelial cells, a critical step in colonization and pathogenesis.
The F17a-A subunit, encoded by the *f17A* gene, is the major structural component of F17 fimbriae. Recombinant F17a-A is produced through genetic engineering, typically by cloning the *f17A* gene into expression vectors (e.g., *E. coli* or yeast systems) to enable large-scale production. The protein retains key functional domains, including the N-terminal lectin-like region responsible for binding to glycosylated receptors, such as mucin-type glycoproteins (e.g., MUC1) on host cells.
Research on F17a-A has focused on its role in host-pathogen interactions, vaccine development, and diagnostic applications. Studies highlight its immunogenicity, making it a candidate for subunit vaccines aimed at preventing E. coli infections in livestock. Additionally, F17a-A-specific antibodies have been explored for diagnostic tools to detect pathogenic E. coli strains.
Recent advances in structural biology have elucidated F17a-A’s binding mechanisms, aiding the design of anti-adhesion therapies. Its recombinant form also serves as a model for studying fimbrial assembly and bacterial adhesion inhibitors. Overall, F17a-A represents a valuable tool for understanding E. coli pathogenesis and developing targeted interventions against enteric infections.
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