| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hly |
| Uniprot No | P09616 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-319aa |
| 氨基酸序列 | ADSDINIKTGTTDIGSNTTVKTGDLVTYDKENGMHKKVFYSFIDDKNHNKKLLVIRTKGTIAGQYRVYSEEGANKSGLAWPSAFKVQLQLPDNEVAQISDYYPRNSIDTKEYMSTLTYGFNGNVTGDDTGKIGGLIGANVSIGHTLKYVQPDFKTILESPTDKKVGWKVIFNNMVNQNWGPYDRDSWNPVYGNQLFMKTRNGSMKAADNFLDPNKASSLLSSGFSPDFATVITMDRKASKQQTNIDVIYERVRDDYQLHWTSTNWKGTNTKDKWTDRSSERYKIDWEKEEMTN |
| 预测分子量 | 33.4 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hly(溶血素)重组蛋白的3篇代表性文献及其摘要内容概括：
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1. **文献名称**：*Cloning and functional characterization of the hemolysin (hly) operon from Escherichia coli*
**作者**：Ludwig, A., & Goebel, W.
**摘要**：本研究首次克隆并表达了来自致病性大肠杆菌的hly操纵子，验证了重组Hly蛋白的溶血活性及细胞毒性，揭示了其依赖钙离子的分泌机制。
2. **文献名称**：*Pore-forming mechanism of Escherichia coli hemolysin (HlyA)*
**作者**：Bhakdi, S., & Tranum-Jensen, J.
**摘要**：通过电镜和生物化学分析，揭示了HlyA蛋白通过寡聚化在宿主细胞膜上形成跨膜孔道的机制，阐明了其导致细胞溶解和炎症反应的分子基础。
3. **文献名称**：*Structural insights into the α-hemolysin toxin from Staphylococcus aureus*
**作者**：Benz, R., Schmid, A., & Dargent, B.
**摘要**：解析了重组表达的α-溶血素(Hly)的跨膜通道结构，探讨了其与宿主细胞膜相互作用的分子机制，为开发靶向抑制剂提供了理论依据。
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以上文献涵盖了hly重组蛋白的基因表达、功能机制及结构研究。如需具体领域(如疫苗开发或临床应用)的文献，可进一步补充说明。
**Background of Hly Recombinant Protein**
Hemolysin (Hly), a pore-forming cytolytic toxin, is a key virulence factor in several pathogenic bacteria, notably *Listeria monocytogenes* and uropathogenic *Escherichia coli* (UPEC). Its primary role is to lyse host cell membranes, facilitating bacterial survival, immune evasion, and tissue invasion. In *L. monocytogenes*, Hly (also called listeriolysin O) enables escape from phagocytic vacuoles, promoting intracellular replication. In UPEC, α-hemolysin disrupts epithelial and immune cells during urinary tract infections.
Recombinant Hly proteins are engineered versions produced via genetic cloning and expression in heterologous systems (e.g., *E. coli* or yeast). This approach allows scalable production while enabling modifications to reduce toxicity or enhance stability. For instance, non-cytotoxic mutants may retain immunogenic epitopes, making them suitable for vaccine development. Recombinant Hly is also used to study host-pathogen interactions, membrane dynamics, and immune responses. Its ability to perforate membranes under controlled conditions has applications in drug delivery and cellular biology research.
Research on Hly has highlighted its dual role as a toxin and a modulator of immune signaling. At sublytic concentrations, it can trigger calcium influx, cytokine release, or NLRP3 inflammasome activation, influencing infection outcomes. These properties make recombinant Hly a valuable tool for dissecting infection mechanisms and designing therapeutic strategies, such as toxoid vaccines or targeted anti-virulence agents. Despite its pathogenic origins, the controlled use of recombinant Hly bridges microbiological research and biomedical innovation.
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