| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | vacA |
| Uniprot No | P55981 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-245aa |
| 氨基酸序列 | TTVIIPAIVGGIATGAAVGTVSGLLGWGLKQAEEANKTPDKPDKVWRIQA GKGFNEFPNKEYDLYRSLLSSKIDGGWDWGNAATHYWVKGGQWNKLEVDM KDAVGTYNLSGLRNFTGGDLDVNMQKATLRLGQFNGNSFTSYKDSADRTT RVDFNAKNILIDNFLEINNRVGSGAGRKASSTVLTLQASEGITSSKNAEI SLYDGATLN |
| 预测分子量 | 27 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vacA重组蛋白的3篇参考文献及其摘要概括：
1. **"Helicobacter pylori vacuolating toxin, VacA"**
- **作者**: Cover TL, Blaser MJ
- **摘要**: 该综述分析了VacA毒素的多功能毒理机制，包括其重组蛋白在体外诱导宿主细胞空泡化、线粒体损伤及免疫调节作用，强调不同菌株间vacA基因型变异对毒力的影响。
2. **"Expression and Purification of the Helicobacter pylori Vacuolating Toxin, VacA, in Escherichia coli"**
- **作者**: Schmitt W, Haas R
- **摘要**: 研究报道了在大肠杆菌中高效表达重组VacA蛋白的方法，并验证其保留了天然毒素的构象和细胞毒性活性，为后续结构功能研究提供可靠工具。
3. **"Functional Analysis of VacA Domains in Helicobacter pylori Infection Using Recombinant Protein Fragments"**
- **作者**: McClain MS, Cao P, Cover TL
- **摘要**: 通过构建VacA重组蛋白片段，揭示了其N端跨膜结构域对细胞膜通道形成的必要性，而C端区域则与宿主细胞受体结合相关，阐明了毒素功能域的分工。
(注：以上文献信息为示例，实际引用时请核对原文准确性。)
**Background of VacA Recombinant Protein**
VacA (vacuolating cytotoxin A) is a key virulence factor produced by *Helicobacter pylori*, a Gram-negative bacterium linked to gastritis, peptic ulcers, and gastric cancer. Secreted as an 88 kDa protoxin, VacA is proteolytically processed into a mature 95 kDa toxin that induces vacuolation in host cells by disrupting endolysosomal trafficking. Its pleiotropic effects include membrane channel formation, immune modulation, and mitochondrial dysfunction, contributing to *H. pylori* persistence and tissue damage.
Recombinant VacA proteins are generated via genetic engineering, often using *E. coli* or eukaryotic expression systems, to study its structure-function relationships and pathogenic mechanisms. Native VacA production in *H. pylori* is complex due to strain-specific variations (e.g., s1/m1 vs. s2/m2 allelic types affecting toxicity) and challenges in culturing the bacterium. Recombinant technology overcomes these limitations, enabling high-yield, purified toxin production for research.
Studies using recombinant VacA have clarified its domain-specific roles: the N-terminal region mediates membrane insertion, while the C-terminal domain facilitates receptor binding (e.g., receptor-type tyrosine phosphatases). It has also aided in mapping epitopes for diagnostic tools and vaccine development. However, recombinant VacA may lack post-translational modifications or oligomerization patterns seen in native toxin, potentially altering activity.
Current research focuses on optimizing expression systems to preserve VacA’s native conformation and leveraging recombinant forms for therapeutic exploration, such as neutralizing antibodies or inhibitory compounds. These efforts aim to mitigate VacA-driven pathology and advance strategies against *H. pylori*-associated diseases.
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