| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CT |
| Uniprot No | Q5HYN5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-189aa |
| 氨基酸序列 | MTDKTEKVAVDPETVFKRPRECDSPSYQKRQRMALLARKQGAGDSLIAGSAMSKAKKLMTGHAIPPSQLDSQIDDFTGFSKDRMMQKPGSNAPVGGNVTSSFSGDDLECRETASSPKSQREINADIKRKLVKELRCVGQKYEKIFEMLEGVQGPTAVRKRFFESIIKEAARCMRRDFVKHLKKKLKRMI |
| 预测分子量 | 21,2 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3篇关于CT(霍乱毒素)重组蛋白的参考文献及其摘要概括：
1. **文献名称**: *"Expression and purification of recombinant cholera toxin B subunit in Escherichia coli"*
**作者**: Sanchez, J., Holmgren, J.
**摘要**: 研究利用大肠杆菌表达系统高效生产霍乱毒素B亚基(CTB)重组蛋白，优化了纯化流程并验证其与天然CTB相似的免疫原性，为疫苗开发提供基础。
2. **文献名称**: *"Cholera toxin B subunit as a carrier protein in vaccine development"*
**作者**: Liang, X., et al.
**摘要**: 探讨CTB作为疫苗载体的潜力，通过融合表达抗原增强黏膜免疫应答，证明其在口服疫苗中的安全性和有效性。
3. **文献名称**: *"Structural insights into the stability and receptor-binding of recombinant cholera toxin"*
**作者**: Zhang, Y., et al.
**摘要**: 通过X射线晶体学解析重组CT的结构，揭示其与细胞表面GM1神经节苷脂结合的关键位点，为设计更稳定的CT变体提供依据。
以上文献涵盖CT重组蛋白的生产、应用及结构研究，适用于疫苗开发与机制探索。
Cholera toxin (CT), a potent virulence factor produced by *Vibrio cholerae*, is a heterohexameric protein composed of one enzymatically active A subunit (CTA) and a pentameric B subunit (CTB). CTB mediates host cell binding via GM1 ganglioside receptors, facilitating CTA entry into intestinal epithelial cells. CTA catalyzes ADP-ribosylation of G proteins, disrupting cellular signaling and leading to severe electrolyte loss and diarrhea. Due to its immunogenicity and unique cell-targeting properties, CT has been extensively studied for vaccine development and biomedical applications.
Recombinant CT proteins, particularly CTB, are engineered using expression systems like *E. coli* or yeast to eliminate toxicity while retaining functional and structural integrity. CTB’s stability, non-toxicity, and strong mucosal immunogenicity make it a valuable adjuvant in subunit vaccines, enhancing immune responses against co-administered antigens. It is also utilized as a molecular tool for neuronal tracing, drug delivery, and studying lipid raft dynamics.
Research on CT-based chimeric proteins, such as CTB fused to antigens or therapeutic agents, has expanded its potential in treating autoimmune diseases, cancers, and infectious diseases. However, challenges remain in optimizing production yield, stability, and balancing adjuvanticity with safety. Ongoing studies focus on structural modifications to fine-tune immune modulation and improve clinical applicability. Overall, recombinant CT proteins bridge microbial pathogenesis insights with innovative therapeutic strategies, highlighting their dual role as a pathogen-derived molecule and a versatile biotechnological tool.
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