| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TCPa |
| Uniprot No | P17987 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-556aa |
| 氨基酸序列 | MEGPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGSYEDAVHSGALND |
| 预测分子量 | 60,3 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. |
以下是关于TCPα重组蛋白的虚构参考文献示例，基于常见研究场景的合理推测：
1. **文献名称**：*Expression and Purification of Recombinant TCPα Protein in Escherichia coli*
**作者**：Smith, J. et al.
**摘要**：本研究报道了利用大肠杆菌表达系统高效生产TCPα重组蛋白的方法，通过优化密码子使用和纯化步骤，获得了高纯度蛋白，并验证了其与配体结合的生物活性。
2. **文献名称**：*Structural Analysis of TCPα Reveals Key Domains for Immune Synapse Formation*
**作者**：Zhang, Y. & Li, H.
**摘要**：通过X射线晶体学解析TCPα重组蛋白的三维结构，发现其N端结构域对T细胞受体信号传导和免疫突触的稳定性具有关键作用，为靶向免疫疗法提供了结构基础。
3. **文献名称**：*Functional Characterization of Recombinant TCPα in Autoimmune Disease Models*
**作者**：Johnson, R. et al.
**摘要**：利用重组TCPα蛋白进行体外实验，证明其可通过调节T细胞活化阈值缓解小鼠自身免疫性疾病症状，提示其作为潜在治疗靶点的价值。
4. **文献名称**：*Plant TCPα Transcription Factor: Recombinant Production and Role in Leaf Development*
**作者**：Chen, L. et al.
**摘要**：在植物学背景下，研究拟南芥TCPα重组蛋白的功能，发现其通过调控细胞分裂相关基因的表达影响叶片形态发生，揭示了其在植物发育中的分子机制。
**备注**：以上文献为假设性示例，实际研究中需根据具体领域(免疫学或植物学)确认TCPα的定义并检索真实文献。若涉及实际科研，建议通过PubMed、Web of Science等数据库查询最新研究。
**Background of TCPα Recombinant Protein**
TCPα (TcpA pilin subunit) is a critical structural protein associated with the type IV pilus (T4P) system in Gram-negative bacteria, notably *Vibrio cholerae*, the causative agent of cholera. The T4P is a filamentous appendage essential for bacterial colonization, biofilm formation, and horizontal gene transfer during infection. TcpA, the primary subunit of the toxin-coregulated pilus, plays a pivotal role in host-pathogen interactions, enabling bacterial attachment to intestinal epithelial cells and facilitating the delivery of virulence factors like cholera toxin.
Recombinant TCPα protein is produced via genetic engineering, typically by cloning the *tcpA* gene into expression vectors (e.g., *E. coli*), followed by purification using affinity chromatography. This approach allows large-scale production of the protein for functional and structural studies. Research on recombinant TCPα has advanced understanding of pilus assembly mechanisms, antigenic properties, and its role in pathogenesis.
Additionally, TCPα is a key target for vaccine development. Antibodies against TcpA can block pilus-mediated adhesion, reducing bacterial colonization. Studies have explored TCPα-based subunit vaccines, often combined with cholera toxin B subunit, to elicit protective mucosal immunity. However, challenges such as antigenic variability and stability under physiological conditions necessitate further optimization.
Beyond vaccinology, recombinant TCPα serves as a tool for investigating bacterial adhesion inhibitors and designing anti-virulence therapies. Its structural analysis via X-ray crystallography or cryo-EM has provided insights into pilin polymerization and dynamics. Overall, TCPα recombinant protein remains integral to both basic microbiological research and translational applications in combating cholera and related infections.
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