| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | fimA |
| Uniprot No | P04128 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-182aa |
| 氨基酸序列 | AATTVNGGTVHFKGEVVNAACAVDAGSVDQTVQLGQVRTASLAQEGATSS AVGFNIQLNDCDTNVASKAAVAFLGTAIDAGHTNVLALQSSAAGSATNVG VQILDRTGAALTLDGATFSSETTLNNGTNTIPFQARYFATGAATPGAANA DATFKVQYQ |
| 预测分子量 | 32 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fimA重组蛋白的3篇参考文献，简要整理如下：
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1. **文献名称**：*Cloning and expression of a *Porphyromonas gingivalis* fimA gene in *Escherichia coli***
**作者**：Y. Ogawa et al.
**摘要**：研究克隆了牙龈卟啉单胞菌(*P. gingivalis*)的fimA基因，并在大肠杆菌中成功表达重组FimA蛋白。通过Western blot验证其抗原性，为开发牙周病相关疫苗提供基础。
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2. **文献名称**：*Immunogenicity of recombinant FimA protein from *Porphyromonas gingivalis* in a murine model***
**作者**：H. Maeba et al.
**摘要**：评估重组FimA蛋白在小鼠模型中的免疫原性，发现其能诱导特异性抗体产生并增强巨噬细胞对细菌的清除能力，提示其在疫苗研发中的潜力。
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3. **文献名称**：*Functional characterization of recombinant FimA in bacterial adhesion and biofilm formation***
**作者**：K. Nakagawa et al.
**摘要**：研究重组FimA蛋白在细菌黏附和生物膜形成中的作用，证实其通过结合宿主细胞表面受体促进致病性，为抗黏附疗法提供理论依据。
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如需具体文献来源(期刊、年份)，可进一步补充关键词或研究背景。
**Background of FimA Recombinant Protein**
FimA, a structural subunit protein of type I fimbriae, plays a critical role in the pathogenesis of several Gram-negative bacteria, notably *Porphyromonas gingivalis* and uropathogenic *Escherichia coli*. These filamentous surface appendages mediate bacterial adherence to host tissues, biofilm formation, and immune evasion, facilitating colonization and infection. In *P. gingivalis*, a keystone pathogen in periodontitis, FimA is essential for binding to salivary proteins, epithelial cells, and extracellular matrix components, triggering inflammatory responses that drive tissue destruction.
Recombinant FimA protein is produced via genetic engineering, where the *fimA* gene is cloned into expression vectors (e.g., *E. coli* or yeast systems) to enable large-scale production. Purification techniques, such as affinity chromatography, yield highly pure FimA for research and therapeutic applications. Its recombinant form retains functional properties, including receptor-binding capacity, making it valuable for studying host-pathogen interactions.
Research on FimA recombinant protein focuses on vaccine development, as it elicits immune responses that block bacterial adhesion. For instance, FimA-based vaccines have shown promise in animal models for preventing periodontal disease or urinary tract infections. Additionally, it serves as a diagnostic antigen to detect pathogen-specific antibodies in clinical samples. Structural studies using recombinant FimA have clarified mechanisms of fimbrial assembly and identified domains critical for virulence, guiding the design of anti-infective agents.
The rise of antibiotic resistance has intensified interest in FimA as a therapeutic target. Inhibitors disrupting FimA-mediated adhesion could prevent infections without promoting resistance. Overall, FimA recombinant protein is a pivotal tool for understanding bacterial virulence and advancing novel antimicrobial strategies.
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