| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | sepA |
| Uniprot No | P0C0Q4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 208-507aa |
| 氨基酸序列 | AATTGTGKGVLGDTKQININSVSGGYALQDLTQQGTLSAYNYDANTGQAYLMQDKDKNFVDDEQRAGVDANYYAKETYDYYKNTFGRESYDNQGSPIISIAHVNNFQGQDNRNNAAWIGDKMIYGDGDGRTFTALSGANDVVAHEITHGVTQQTANLVYRSQSGALNESFSDVFGYFIDDEDFLMGEDVYTPGVGGDALRSMSNPERFGQPSHMNDFVYTNSDNGGVHTNSGIPNKAAYNTIRSIGKQRSEQIYYRALTVYLTSNSDFQDAKASLQQAAFDLYGDGIAQQVGQAWDSVGV |
| 预测分子量 | 37.7 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 **sepA 重组蛋白**的3篇参考文献及其摘要概括：
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1. **文献名称**：*Cloning and characterization of the secreted protease SepA from *Shigella flexneri**
**作者**：Hirose K, et al.
**摘要**：该研究克隆了痢疾志贺氏菌(*Shigella flexneri*)的 *sepA* 基因，并在大肠杆菌中成功表达重组SepA蛋白。研究发现SepA是一种丝氨酸蛋白酶，可能参与细菌的宿主细胞侵袭及胞外基质的降解。
2. **文献名称**：*Structural and functional analysis of the SepA protease in bacterial pathogenesis*
**作者**：Al-Hasani K, et al.
**摘要**：通过X射线晶体学解析了重组SepA的三维结构，揭示了其底物结合域和催化机制。实验表明，SepA通过切割宿主细胞间连接蛋白(如occludin)促进病原菌的肠道黏膜屏障破坏。
3. **文献名称**：*Recombinant SepA as a potential vaccine candidate against *Salmonella* infection*
**作者**：Souza A, et al.
**摘要**：评估了重组SepA蛋白在小鼠模型中的免疫原性，发现其能诱导Th1/Th17免疫反应，显著降低沙门氏菌(*Salmonella*)感染的细菌载量，提示其作为疫苗抗原的潜力。
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以上文献示例基于类似领域研究整合而成，具体内容需根据实际文献调整。如需真实文献，建议通过PubMed或Google Scholar检索关键词“sepA recombinant protein”、“SepA protease function”等。
**Background of SepA Recombinant Protein**
SepA is a large multidomain protein initially identified in *Shigella flexneri*, a Gram-negative bacterium responsible for bacillary dysentery. It belongs to the family of serine protease autotransporters (SPATEs), which are virulence factors secreted by pathogenic *Enterobacteriaceae*. SepA plays a critical role in bacterial pathogenesis, contributing to host tissue invasion, immune evasion, and colonization. Structurally, it contains a protease domain with a catalytic serine residue and a C-terminal β-barrel domain facilitating its autotranslocation across the bacterial outer membrane.
The recombinant SepA protein is engineered for research and therapeutic applications. By cloning the *sepA* gene into expression vectors (e.g., *E. coli* systems), researchers produce purified SepA to study its enzymatic activity, substrate specificity, and interactions with host proteins. Studies reveal that SepA cleaves mucin, extracellular matrix components, and immunomodulatory peptides, promoting bacterial dissemination and dampening host inflammatory responses.
Interest in SepA also stems from its potential as a vaccine candidate or diagnostic marker. Mutational analyses highlight residues critical for protease activity, guiding the design of inhibitors to block its function. Additionally, recombinant SepA aids in elucidating structural features through X-ray crystallography and cryo-EM, providing insights into SPATE mechanisms.
Despite progress, questions remain about its precise role in infection dynamics and cross-talk with other virulence factors. Ongoing research leverages recombinant SepA to address these gaps, aiming to develop targeted anti-infective strategies against *Shigella* and related pathogens.
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