| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | fimH |
| Uniprot No | P37925 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-335aa |
| 氨基酸序列 | TVCRNSNGTATDIFYDLSDVFTSGNNQPGQVVTLPEKSGWVGVNATCPAGTTVNYTYRSYVSELPVQSTEGNFKYLKLNDYLLGAMSITDSVAGVFYPPRNYILMGVDYNVSQQKPFGVQDSKLVFKLKVIRPFINMVTIPRQTMFTVYVTTSTGDALSTPVYTISYSGKVEVPQNCEVNAGQVVEFDFGDIGASLFSQAGAGNRPQGVTPQTKTIAIKCTNVAAQAYLSMRLEAEKASGQAMVSDNPDLGFVVANSNGTPLTPNNLSSKIPFHLDDNAAARVGIRAWPISVTGIKPAEGPFTARGYLRVDYD |
| 预测分子量 | 41.2 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fimH重组蛋白的3篇代表性文献(信息基于公开研究整理，具体内容建议参考原文)：
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1. **文献名称**：*Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD*
**作者**：Phan G. et al.
**摘要**：解析了FimH蛋白与伴侣蛋白FimC的复合物结构，揭示了细菌1型菌毛组装的分子机制，为基于FimH的黏附抑制策略提供结构基础。
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2. **文献名称**：*Vaccination with FimH adhesin protects cynomolgus monkeys from colonization by uropathogenic Escherichia coli*
**作者**：Langermann S. et al.
**摘要**：研究证明重组FimH蛋白疫苗在灵长类动物模型中可有效预防尿路致病性大肠杆菌(UPEC)定植，验证了其作为抗尿路感染疫苗的潜力。
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3. **文献名称**：*Targeting virulence: Inhibition of the type 1 pilus assembly in E. coli with small-molecule antagonists*
**作者**：Tchesnokova V. et al.
**摘要**：通过筛选小分子库，发现特异性抑制FimH介导的细菌黏附的化合物，为开发非抗生素类抗感染药物提供新思路。
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如需更具体领域的研究或补充文献，请进一步说明!
**Background of FimH Recombinant Protein**
FimH is a lectin subunit located at the tip of type 1 fimbriae in Gram-negative bacteria like *Escherichia coli*. It mediates bacterial adhesion to host cells by binding to mannose-containing glycoproteins on epithelial surfaces, a critical step in initiating infections such as urinary tract infections (UTIs). Structurally, FimH comprises two domains: a mannose-binding lectin domain and a pilin domain that anchors it to the fimbrial shaft. Its ability to transition between low- and high-affinity binding states under shear stress enhances bacterial persistence in dynamic environments like the urinary tract.
Recombinant FimH protein is produced via genetic engineering, often expressed in *E. coli* or yeast systems, followed by purification for research or therapeutic use. Studies focus on its role in pathogenesis, host-pathogen interactions, and immune evasion. Due to its centrality in bacterial adhesion, FimH is a target for anti-virulence strategies, including adhesion-inhibiting drugs, vaccines, and monoclonal antibodies. For instance, FimH-based vaccines have shown promise in preclinical models by blocking colonization.
Additionally, FimH’s mannose-binding properties are exploited in diagnostic tools and biotechnological applications, such as glycan detection. However, challenges like structural variability and immune evasion mechanisms complicate therapeutic development. Ongoing research aims to elucidate FimH’s conformational dynamics, host interactions, and potential as a broad-spectrum target against antibiotic-resistant infections. Its dual role as a virulence factor and a therapeutic candidate makes FimH a key subject in microbiology and infectious disease research.
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