| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | zot |
| Uniprot No | P38442 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-399aa |
| 氨基酸序列 | MSIFIHHGAPGSYKTSGALWLRLLPAIKSGRHIITNVRGLNLERMAKYLKMDVSDISIEFIDTDHPDGRLTMARFWHWARKDAFLFIDECGRIWPPRLTVTNLKALDTPPDLVAEDRPESFEVAFDMHRHHGWDICLTTPNIAKVHNMIREAAEIGYRHFNRATVGLGAKFTLTTHDAANSGQMDSHALTRQVKKIPSPIFKMYASTTTGKARDTMAGTALWKDRKILFLFGMVFLMFSYSFYGLHDNPIFTGGNDATIESEQSEPQSKATVGNAVGSKAVAPASFGFCIGRLCVQDGFVTVGDERYRLVDNLDIPYRGLWATGHHIYKDTLTVFFETESGSVPTELFASSYRYKVLPLPDFNHFVVFDTFAAQALWVEVKRGLPIKTENDKKGLNSIF |
| 预测分子量 | 46.9 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ZOT重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Zonula occludens toxin (ZOT) as a novel tool for drug delivery*
**作者**：Fasano A., Uzzau S.
**摘要**：该研究首次揭示了霍乱弧菌分泌的ZOT蛋白通过可逆调节肠道上皮细胞紧密连接，增强大分子药物的跨膜吸收。作者提出重组ZOT可作为生物递送增强剂，并验证了其在动物模型中的有效性。
2. **文献名称**：*Recombinant ZOT-derived peptide improves oral insulin delivery in diabetic mice*
**作者**：Salama N.N., Fasano A.
**摘要**：研究团队利用重组ZOT蛋白片段设计合成肽，证明其可通过激活细胞内吞作用促进胰岛素的口服吸收。实验显示该肽能显著降低糖尿病小鼠血糖水平，且无黏膜毒性。
3. **文献名称**：*Mechanistic insights into ZOT-induced tight junction modulation*
**作者**：Watson C.J., Rowland M.
**摘要**：通过体外肠上皮细胞模型，揭示了重组ZOT蛋白通过激活PKCζ信号通路导致紧密连接蛋白occludin重分布，从而短暂增加细胞旁通透性，为精准控制药物递送时间窗提供理论依据。
Zonula Occludens Toxin (ZOT), a protein initially identified in *Vibrio cholerae*, plays a critical role in the pathogenicity of cholera by modulating intestinal epithelial barrier function. Discovered in the 1990s, ZOT selectively increases paracellular permeability of the small intestine by interacting with eukaryotic cell receptors, particularly targeting tight junction complexes. This activity facilitates bacterial dissemination and toxin delivery, contributing to the severe diarrhea characteristic of cholera infection.
Structurally, ZOT contains distinct functional domains: an N-terminal region involved in proteolytic processing, a central receptor-binding domain, and a C-terminal domain critical for toxin secretion. Research revealed that ZOT’s mechanism involves binding to cell surface receptors such as zonulin and epidermal growth factor receptor (EGFR), triggering intracellular signaling cascades that reorganize cytoskeletal proteins (e.g., occludin, ZO-1) and destabilize tight junctions. Interestingly, this property has been repurposed for biomedical applications. Recombinant ZOT, particularly its biologically active fragment ΔG (lacking the N-terminal domain), has emerged as a tool to reversibly enhance epithelial and endothelial permeability. This capability is exploited in drug delivery systems to improve absorption of therapeutics, including macromolecules and nanoparticles, across biological barriers like the blood-brain barrier or intestinal mucosa.
Current studies focus on optimizing ZOT-derived peptides for clinical use, balancing efficacy with safety to avoid unintended immune responses or prolonged barrier disruption. Its potential extends to treating conditions involving excessive barrier integrity, such as inflammatory bowel disease or certain neurological disorders. However, further research is needed to fully elucidate its long-term effects and refine its therapeutic applications.
×
