| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VCC1 |
| Uniprot No | Q6UXB2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-119aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL |
| 预测分子量 | 14 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VCC1(Vibrio cholerae cytolysin 1)重组蛋白的3篇代表性文献摘要：
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1. **文献名称**: *"Structural basis of Vibrio cholerae cytolysin assembly and membrane pore formation"*
**作者**: De S, et al.
**摘要**: 该研究通过冷冻电镜解析了VCC1毒素的寡聚体结构，揭示了其与胆固醇结合后形成跨膜β桶状孔道的分子机制，阐明了其溶血活性的结构基础。
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2. **文献名称**: *"Recombinant expression and functional characterization of the pore-forming toxin VCC from Vibrio cholerae"*
**作者**: Zitzer A, et al.
**摘要**: 报道了在大肠杆菌中重组表达并纯化VCC1蛋白的方法，通过体外溶血实验和脂质体渗透性分析，证实重组蛋白具有与天然毒素相似的生物活性。
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3. **文献名称**: *"Vibrio cholerae cytolysin induces apoptosis in intestinal epithelial cells via mitochondrial membrane depolarization"*
**作者**: Mitra R, et al.
**摘要**: 研究发现重组VCC1通过破坏细胞膜完整性导致线粒体膜电位崩溃，进而激活Caspase通路引发细胞凋亡，揭示了其双重细胞毒性机制。
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注：以上文献信息为示例，实际研究中建议通过PubMed或Web of Science以“Vibrio cholerae cytolysin”或“VCC toxin recombinant”为关键词检索最新论文。
VCC1 (Vibrio cholerae cytolysin 1), also known as hemolysin HlyA, is a pore-forming toxin produced by the pathogenic bacterium *Vibrio cholerae*, the causative agent of cholera. While cholera is primarily associated with the devastating diarrheal disease triggered by the cholera toxin (CTX), VCC1 contributes to the pathogen’s virulence by damaging host cells and modulating immune responses. This 82-kDa protein belongs to the repeats-in-toxin (RTX) family and exhibits calcium-dependent cytolytic activity against erythrocytes, epithelial cells, and immune cells.
Structurally, VCC1 contains a β-barrel pore-forming domain and a lectin-like domain that facilitates binding to specific glycosphingolipid receptors on host membranes. Upon attachment, it oligomerizes to form transmembrane pores, disrupting ion gradients and inducing cell lysis or apoptosis. Beyond direct cytotoxicity, VCC1 activates pro-inflammatory pathways and compromises epithelial barrier integrity, potentially enhancing bacterial dissemination. Its role in cholera pathogenesis remains under investigation, but studies suggest it may synergize with CTX by exacerbating intestinal inflammation or facilitating bacterial survival in host niches.
Recombinant VCC1 is produced via heterologous expression systems (e.g., *E. coli*) for functional and structural studies. Purification typically involves affinity chromatography tags (e.g., His-tag) and refolding steps to maintain activity. Researchers utilize recombinant VCC1 to dissect its mechanism of membrane perforation, host-cell interactions, and immunomodulatory effects. It also serves as a tool to explore pore-forming toxin biology or screen inhibitory compounds for therapeutic development. However, its cytotoxic nature limits its direct use in vaccines, prompting interest in engineered attenuated variants. Overall, VCC1 exemplifies how bacterial toxins balance destructive and immune-evasive functions, offering insights into both cholera pathology and broader host-pathogen dynamics.
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