| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | fimC |
| Uniprot No | P31697 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-241aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGVALGATRVIYPAGQKQEQLAVTNNDENS TYLIQSWVENADGVKDGRFIVTPPLFAMKGKKENTLRILDATNNQLPQDR ESLFWMNVKAIPSMDKSKLTENTLQLAIISRIKLYYRPAKLALPPDQAAE KLRFRRSANSLTLINPTPYYLTVTELNAGTRVLENALVPPMGESTVKLPS DAGSNITYRTINDYGALTPKMTGVME |
| 预测分子量 | 25 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fimC重组蛋白的参考文献示例(注：内容基于研究领域常见主题构造，具体文献请以实际检索为准)：
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1. **文献名称**: *Cloning and expression of the fimC gene encoding the chaperone protein of Escherichia coli type 1 fimbriae*
**作者**: Choudhury, D. et al.
**摘要**: 研究报道了fimC基因在大肠杆菌中的克隆及重组蛋白表达，通过优化表达条件获得可溶性FimC蛋白，并验证其作为伴侣蛋白在菌毛组装中的功能。
2. **文献名称**: *Structural insights into FimC-mediated pilus biogenesis in uropathogenic E. coli*
**作者**: Sauer, M.M. et al.
**摘要**: 利用X射线晶体学解析FimC与菌毛亚基FimH的复合物结构，阐明FimC通过结合未折叠的FimH促进菌毛形成的分子机制。
3. **文献名称**: *Recombinant FimC as a potential vaccine candidate against urinary tract infections*
**作者**: Wurpel, D.J. et al.
**摘要**: 评估重组FimC蛋白在小鼠模型中的免疫保护效果，表明其可诱导特异性抗体并减少致病性大肠杆菌的膀胱定植。
4. **文献名称**: *Functional characterization of FimC in bacterial adhesion and biofilm formation*
**作者**: Jones, C.H. et al.
**摘要**: 通过基因敲除和重组蛋白回补实验，证实FimC缺失导致菌毛组装缺陷，并显著降低细菌对宿主细胞的粘附及生物膜形成能力。
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建议通过PubMed或Web of Science以“fimC recombinant protein”为关键词检索最新文献获取准确信息。
FimC is a periplasmic chaperone protein critically involved in the assembly of type 1 pili in *Escherichia coli* and other Gram-negative bacteria. These hair-like surface appendages mediate bacterial adhesion to host cells, a key step in initiating infections. The chaperone-usher pathway responsible for pilus biogenesis relies on FimC to ensure proper folding, stabilization, and transport of pilus subunits (e.g., FimA, FimH) across the periplasmic space. FimC achieves this by binding to nascent subunit proteins via a conserved "chaperone cleft," shielding hydrophobic regions that might otherwise cause aggregation. This interaction also facilitates the delivery of subunits to the outer membrane usher protein FimD for final pilus polymerization.
Recombinant FimC (rFimC) is engineered for laboratory studies, typically expressed in heterologous systems like *E. coli* or mammalian cells. Its production enables detailed structural and functional analyses, including X-ray crystallography and binding assays, to dissect molecular mechanisms of pilus assembly. Researchers leverage rFimC to investigate host-pathogen interactions, particularly how FimH adhesins mediate attachment to urinary tract epithelia, a process linked to urinary tract infections (UTIs). Additionally, rFimC serves as a tool in developing anti-adhesion therapies, such as small-molecule inhibitors or antibodies targeting the FimC-FimH interface to block bacterial colonization.
Beyond pathogenesis studies, rFimC has applications in vaccine development, where pilus components are explored as immunogens. Its role in biofilm formation also makes it relevant in studying antimicrobial resistance and surface colonization strategies. By enabling controlled in vitro reconstitution of pilus assembly steps, rFimC remains pivotal for advancing both basic microbiology and translational research aimed at combating bacterial infections.
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