| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | fimG |
| Uniprot No | P08190 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-167aa |
| 氨基酸序列 | ADVTITVNGKVVAKPCTVSTTNATVDLGDLYSFSLMSAGAASAWHDVALELTNCPVGTSRVTASFSGAADSTGYYKNQGTAQNIQLELQDDSGNTLNTGATKTVQVDDSSQSAHFPLQVRALTVNGGATQGTIQAVISITYTYS |
| 预测分子量 | 22.3 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3-4条关于 **fimG重组蛋白** 的参考文献示例(内容为模拟虚构，仅供参考)：
1. **文献名称**：*"Recombinant expression and functional analysis of FimG in Escherichia coli biofilm formation"*
**作者**：Chen L. et al.
**摘要**：研究通过重组技术表达fimG蛋白，并证实其在细菌生物膜形成中的关键作用。通过基因敲除和回补实验，发现重组FimG能恢复突变菌株的黏附能力。
2. **文献名称**：*"Structural characterization of FimG using X-ray crystallography and its implications in pilus assembly"*
**作者**：Watanabe K. et al.
**摘要**：解析了重组FimG蛋白的晶体结构，揭示了其与菌毛其他组分(如FimF)的相互作用界面，为理解I型菌毛的组装机制提供结构基础。
3. **文献名称**：*"Development of a FimG-based inhibitor against urinary tract infections"*
**作者**：Singh R. et al.
**摘要**：利用重组FimG蛋白筛选小分子抑制剂，阻断病原菌与宿主细胞的黏附，为治疗尿路感染提供潜在策略。
4. **文献名称**：*"Comparative analysis of FimG homologs in Enterobacteriaceae: implications for host specificity"*
**作者**：Müller S. et al.
**摘要**：通过重组表达不同菌属的FimG蛋白，比较其序列和功能差异，发现其与宿主细胞受体结合的物种特异性机制。
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如需真实文献，建议通过 **PubMed/Google Scholar** 检索关键词：`"fimG recombinant"` 或 `"FimG protein structure/function"`。
**Background of Recombinant FimG Protein**
FimG is a subunit protein found in type 1 fimbriae, hair-like adhesive structures expressed by *Escherichia coli* and other Gram-negative bacteria. These fimbriae play a critical role in bacterial adhesion to host surfaces, facilitating colonization and infection. The type 1 fimbrial structure is primarily composed of the major subunit FimA, which forms the filament, and minor subunits (FimF, FimG, and FimH) located at the tip. FimH acts as the adhesin, binding to mannose-containing receptors on host cells, while FimG is proposed to act as an adaptor, stabilizing the tip complex and mediating proper assembly of the fimbrial structure.
Recombinant FimG refers to the protein produced via genetic engineering, often expressed in heterologous systems like *E. coli* or yeast. This approach enables large-scale production of purified FimG for functional and structural studies. Research on recombinant FimG has focused on elucidating its role in fimbrial biogenesis, host-pathogen interactions, and potential as a therapeutic target. Studies suggest that FimG contributes to the stability of the FimH-FimF-G tip complex, ensuring optimal orientation of FimH for host receptor binding.
Interest in recombinant FimG also stems from its potential applications in anti-virulence strategies. Inhibiting FimG-mediated assembly could disrupt fimbrial function, reducing bacterial adhesion and infection. Additionally, recombinant FimG serves as a tool for antibody production, structural analysis (e.g., X-ray crystallography), and vaccine development. Its study provides insights into bacterial pathogenesis and aids in designing novel interventions against antibiotic-resistant infections.
Overall, recombinant FimG is a key focus in understanding bacterial adhesion mechanisms and developing targeted antimicrobial therapies.
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