| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hlyE |
| Uniprot No | P77335 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-182aa |
| 氨基酸序列 | TEIVADKTVEVVKNAIETADGALDLYNKYLDQVIPWQTFDETIKELSRFKQEYSQAASVLVGDIKTLLMDSQDKYFEATQTVYEWCGVATQLLAAYILLFDEYNEKKASAQKDILIKVLDDGITKLNEAQKSLLVSSQSFNNASGKLLALDSQLTNDFSEKSSYFQSQVDKIRKEAYAGAA |
| 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. |
以下是关于hlyE重组蛋白的3篇参考文献及其摘要概括：
---
1. **文献名称**：*"Cloning, expression, and purification of the hemolysin E protein from Escherichia coli"*
**作者**：Smith A, et al.
**摘要**：本研究成功在大肠杆菌表达系统中克隆并纯化了重组hlyE蛋白，验证其溶血活性，并证明其通过形成跨膜孔破坏宿主细胞膜结构。
2. **文献名称**：*"Structural and functional analysis of the pore-forming toxin hlyE"*
**作者**：Chen L, et al.
**摘要**：通过X射线晶体学解析重组hlyE蛋白的三维结构，揭示了其独特的β-桶状孔形成机制，并发现其溶血活性依赖特定的pH环境。
3. **文献名称**：*"Recombinant hlyE as a potential vaccine candidate against pathogenic E. coli infections"*
**作者**：Wang Y, et al.
**摘要**：评估重组hlyE蛋白在小鼠模型中的免疫原性，发现其能诱导保护性抗体反应，为开发抗大肠杆菌感染的亚单位疫苗提供依据。
---
**备注**：上述文献为示例性内容，实际引用需根据具体研究补充真实发表信息。如需精确文献，建议通过PubMed或Web of Science检索关键词(如“hlyE recombinant protein”或“hemolysin E expression”)。
**Background of HlyE Recombinant Protein**
HlyE (hemolysin E) is a pore-forming cytolytic toxin initially identified in *Escherichia coli* and other Enterobacteriaceae. It belongs to the α-helical pore-forming toxin family, characterized by its ability to oligomerize and form transmembrane channels in host cell membranes, leading to osmotic lysis. Unlike other bacterial hemolysins (e.g., HlyA of *E. coli*), HlyE lacks a typical signal peptide and is secreted via a poorly understood mechanism, possibly involving outer membrane vesicles or specific chaperones. Its gene, *hlyE* (or *sheA*), is often regulated by environmental stressors like oxidative stress or anaerobic conditions, suggesting a role in bacterial survival or pathogenesis.
Recombinant HlyE (rHlyE) is produced through genetic engineering, typically by cloning the *hlyE* gene into expression vectors (e.g., *E. coli* or yeast systems) for large-scale purification. Studies highlight its significance as a virulence factor in bacterial infections, contributing to host cell damage, immune evasion, and biofilm formation. rHlyE serves as a tool to dissect its structure-function relationships, including membrane interaction mechanisms and pore assembly dynamics. Structural analyses reveal a unique "saddle-shaped" dimeric conformation that undergoes conformational changes to penetrate lipid bilayers.
In biotechnology, rHlyE is explored for vaccine development, as antibodies against HlyE can neutralize its cytotoxic effects, offering potential protection against pathogenic strains. It also aids in studying bacterial-host interactions, drug screening for pore-forming toxin inhibitors, and engineered delivery systems for targeted cell lysis. However, challenges remain in optimizing its solubility and stability during recombinant production, as native HlyE tends to aggregate. Advances in protein engineering, such as fusion tags or mutagenesis, have improved its applicability in research and therapeutic contexts.
Overall, rHlyE exemplifies how bacterial toxins, once understood, can be repurposed into valuable tools for both basic science and biomedical innovation.
×
