首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LT |
| Uniprot No | P01860 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 99-377aa |
| 氨基酸序列 | ELKTPLGDTT HTCPRCPEPK SCDTPPPCPR CPEPKSCDTP PPCPRCPEPK SCDTPPPCPR CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVQFKWY VDGVEVHNAK TKPREEQYNS TFRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK TKGQPREPQV YTLPPSREEM TKNQVSLTCL VKGFYPSDIA VEWESSGQPE NNYNTTPPML DSDGSFFLYS KLTVDKSRWQ QGNIFSCSVM HEALHNRFTQ KSLSLSPGK |
| 预测分子量 | 31 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LT(大肠杆菌热不稳定肠毒素)重组蛋白的经典文献摘要概括，供参考：
---
1. **文献名称**：*"Escherichia coli heat-labile enterotoxin: Structure and function of a potent oral adjuvant"*
**作者**：Holmgren J, et al.
**摘要**：该综述系统总结了LT的结构特征及其作为黏膜疫苗佐剂的机制，重点解析了其通过结合GM1神经节苷脂激活免疫细胞的分子机制，并探讨了突变体(如LTK63)在降低毒性同时保留佐剂活性的应用前景。
2. **文献名称**：*"Genetic detoxification of bacterial toxins: A new approach to vaccine development"*
**作者**：Pizza M, et al.
**摘要**：研究团队通过基因工程手段对LT的A亚基进行关键位点突变(如Arg192Gly)，成功获得无毒性但保留免疫原性的重组LT蛋白(LTK63)，实验证明其在小鼠模型中可显著增强抗原特异性抗体和T细胞应答。
3. **文献名称**：*"Crystal structure of the LT complex with a GM1 ganglioside analog"*
**作者**：Merritt EA, et al.
**摘要**：通过X射线晶体学解析了LT五聚体与宿主细胞表面受体GM1的复合物结构，揭示了B亚基与GM1糖基的精确结合模式，为设计靶向性更强的重组LT载体提供了结构基础。
---
**说明**：LT重组蛋白的研究主要集中在疫苗佐剂开发(如增强黏膜免疫)、结构功能解析(毒素-受体互作)及毒性改造(突变体应用)。以上文献涵盖机制、工程应用和结构生物学三个方向，如需具体年份或DOI可进一步补充。
**Background of LT Recombinant Protein**
The LT (labile toxin) recombinant protein is derived from the heat-labile enterotoxin produced by *Escherichia coli* (ETEC), a major causative agent of bacterial diarrhea. Native LT is a heterohexameric protein composed of one enzymatically active A subunit (LTA) and a pentameric B subunit (LTB). LTA exhibits ADP-ribosyltransferase activity, modifying host cell proteins to disrupt cellular signaling, while LTB mediates toxin binding to host cell surface receptors, particularly gangliosides.
In the 1980s, researchers recognized LT’s potential as a mucosal adjuvant due to its ability to enhance immune responses to co-administered antigens. Unlike traditional adjuvants, LT stimulates both systemic and mucosal immunity, making it valuable for vaccines targeting respiratory, gastrointestinal, or urogenital pathogens. However, native LT’s inherent toxicity limited its clinical use. This led to the development of recombinant LT variants with reduced toxicity but retained adjuvant properties. For example, LTK63 (a serine-to-lysine mutant in LTA) and LTR72 (an alanine-to-arginine mutant) are well-studied derivatives that minimize enzymatic activity while preserving immunostimulatory effects.
Recombinant LT proteins are typically produced using *E. coli* or mammalian expression systems, enabling scalable and cost-effective manufacturing. Their applications span preclinical and clinical vaccine research, including efforts against influenza, HPV, and Helicobacter pylori. Additionally, LTB alone has been explored as a non-toxic antigen carrier or targeting moiety in conjugate vaccines. Ongoing studies focus on optimizing LT-based adjuvants for safety and efficacy, highlighting their role in advancing next-generation mucosal vaccines.
×
