| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pilA |
| 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 | AATTVNGGTVHFKGEVVNAACAVDAGSVDQTVQLGQVRTASLAQEGATSSAVGFNIQLNDCDTNVASKAAVAFLGTAIDAGHTNVLALQSSAAGSATNVGVQILDRTGAALTLDGATFSSETTLNNGTNTIPFQARYFATGAATPGAANADATFKVQYQ |
| 预测分子量 | 31.8kDa |
| 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 **pilA重组蛋白** 的3篇参考文献及其摘要内容简述：
1. **《Cloning and expression of the Pseudomonas aeruginosa pilA gene in Escherichia coli》**
- **作者**: Mattick, J.S. et al.
- **摘要**: 研究报道了铜绿假单胞菌中 **pilA基因** 的克隆及在大肠杆菌中的重组表达，证实重组PilA蛋白可自组装成类似天然菌毛的结构，为研究菌毛的黏附功能提供基础。
2. **《Immunogenicity of recombinant PilA protein in a murine model of Pseudomonas aeruginosa infection》**
- **作者**: Lee, K.K. et al.
- **摘要**: 评估重组PilA蛋白作为疫苗候选的潜力，实验表明接种后的小鼠对铜绿假单胞菌感染具有显著保护作用，提示PilA在免疫防御中的关键作用。
3. **《Structural characterization of the Pseudomonas aeruginosa type IV pilus subunit PilA》**
- **作者**: Craig, L. et al.
- **摘要**: 通过X射线晶体学解析重组PilA蛋白的三维结构，揭示其N端受体结合域的结构特征，解释了菌毛在宿主细胞黏附和生物膜形成中的分子机制。
以上均为虚构示例，实际文献需通过PubMed或Google Scholar检索关键词(如“recombinant PilA protein”)获取。
**Background of PilA Recombinant Protein**
PilA, a key structural subunit of bacterial type IV pili (T4P), plays critical roles in microbial adhesion, biofilm formation, motility, and host-pathogen interactions. Primarily studied in pathogens like *Pseudomonas aeruginosa* and *Neisseria gonorrhoeae*, PilA forms filamentous appendages that enable surface attachment, DNA uptake (natural competence), and virulence. Its immunogenic properties and involvement in infection mechanisms make it a target for therapeutic and diagnostic research.
Recombinant PilA is produced via genetic engineering, typically by cloning the *pilA* gene into expression vectors (e.g., *E. coli* or yeast systems) followed by purification using affinity chromatography. This approach allows large-scale production of the protein while retaining its native structure and antigenicity. Researchers often modify expression conditions (e.g., induction temperature, solubility tags) to address challenges like protein aggregation or misfolding.
Studies on recombinant PilA focus on understanding pilus assembly, host immune responses, and its potential as a vaccine candidate. For instance, PilA-based vaccines have shown promise in animal models by eliciting antibodies that block bacterial adhesion. Additionally, recombinant PilA serves as a tool to dissect molecular mechanisms of antibiotic resistance and biofilm-related infections. Recent advances in structural biology, such as cryo-EM, have further clarified PilA’s conformational dynamics and interactions with host cells.
Despite progress, variability in PilA sequences across bacterial strains and post-translational modifications (e.g., glycosylation in *P. aeruginosa*) complicate universal applications. Ongoing research aims to optimize expression systems and engineer chimeric or conserved epitopes to enhance cross-protective efficacy. Overall, PilA recombinant protein remains a vital resource for both basic microbiology and translational innovation.
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