| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ipaB |
| Uniprot No | P18011 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-580aa |
| 氨基酸序列 | MHNVSTTTTGFPLAKILTSTELGDNTIQAANDAANKLFSLTIADLTANQNINTTNAHSTSNILIPELKAPKSLNASSQLTLLIGNLIQILGEKSLTALTNKITAWKSQQQARQQKNLEFSDKINTLLSETEGLTRDYEKQINKLKNADSKIKDLENKINQIQTRLSELDPESPEKKKLSREEIQLTIKKDAAVKDRTLIEQKTLSIHSKLTDKSMQLEKEIDSFSAFSNTASAEQLSTQQKSLTGLASVTQLMATFIQLVGKNNEESLKNDLALFQSLQESRKTEMERKSDEYAAEVRKAEELNRVMGCVGKILGALLTIVSVVAAAFSGGASLALAAVGLALMVTDAIVQAATGNSFMEQALNPIMKAVIEPLIKLLSDAFTKMLEGLGVDSKKAKMIGSILGAIAGALVLVAAVVLVATVGKQAAAKLAENIGKIIGKTLTDLIPKFLKNFSSQLDDLITNAVARLNKFLGAAGDEVISKQIISTHLNQAVLLGESVNSATQAGGSVASAVFQNSASTNLADLTLSKYQVEQLSKYISEAIEKFGQLQEVIADLLASMSNSQANRTDVAKAILQQTTA |
| 预测分子量 | 62,2 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ipaB重组蛋白的3篇参考文献及其摘要概述：
1. **"Identification of a Shigella flexneri recombinant epitope expressing IpaB and IpaD proteins recognized by antibodies in serum of convalescent shigellosis patients"**
- **作者**: Turbyfill et al.
- **摘要**: 该研究评估了重组表达的IpaB和IpaD蛋白作为志贺氏菌疫苗候选的潜力，证明其在小鼠模型中可诱导特异性抗体反应，并提供对细菌攻击的保护作用。
2. **"IpaB from Shigella and SipB from Salmonella utilize similar mechanisms to translocate host cell membranes and induce inflammasome activation"**
- **作者**: Espina et al.
- **摘要**: 通过重组IpaB蛋白实验，揭示了志贺氏菌IpaB通过形成孔道结构介导细菌效应蛋白向宿主细胞的转运，并激活宿主炎性小体通路，促进IL-1β分泌。
3. **"Shigella type III secretion protein MxiI is recognized by Naip2 to induce Nlrc4 inflammasome activation independently of Pkcsδ"**
- **作者**: Suzuki et al.
- **摘要**: 研究发现重组IpaB蛋白与宿主Naip蛋白互作，触发Nlrc4炎性小体组装，进而激活caspase-1.揭示了志贺氏菌感染中宿主免疫应答的分子机制。
4. **"Structural insights into the assembly of the type III secretion needle complex using recombinant IpaB-IpgC complex"**
- **作者**: Blocker et al.
- **摘要**: 利用重组IpaB与其伴侣蛋白IpgC的复合物进行结构分析，阐明了III型分泌系统针状复合体的组装机制，为靶向毒力因子的药物设计提供依据。
以上文献涵盖疫苗开发、宿主-病原体互作及结构机制研究，均为重组IpaB蛋白功能研究的关键工作。
IpaB is a critical virulence factor produced by *Shigella* species, the causative agents of shigellosis (bacillary dysentery). It is a component of the type III secretion system (T3SS), a needle-like apparatus used by *Shigella* to inject effector proteins into host cells during infection. IpaB plays a dual role: it forms the translocon pore in the host cell membrane, facilitating the delivery of other effector proteins, and acts as a chaperone for IpaC, stabilizing its partner protein prior to secretion. Additionally, IpaB is involved in inducing pyroptosis, a pro-inflammatory cell death pathway that contributes to the inflammatory response characteristic of shigellosis.
Recombinant IpaB protein is produced through genetic engineering, typically using *E. coli* expression systems. By cloning the *ipaB* gene into expression vectors, researchers can produce purified IpaB for functional and structural studies. This recombinant protein has been instrumental in elucidating *Shigella* invasion mechanisms, host-pathogen interactions, and immune evasion strategies. Studies using recombinant IpaB have revealed its role in caspase-1 activation, inflammasome signaling, and intracellular survival of the pathogen.
The protein is also a candidate for vaccine development. Antibodies against IpaB show neutralizing effects, and its inclusion in subunit vaccines has been explored to induce protective immunity. However, challenges such as protein stability, proper folding, and immune recognition persist. Recent advances in structural biology and adjuvant technologies have revitalized interest in IpaB as a therapeutic target. Research continues to focus on optimizing recombinant IpaB production and understanding its conformational epitopes to design novel interventions against *Shigella* infections, which remain a significant global health burden, particularly in low-resource settings.
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