| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | mcjB |
| Uniprot No | Q9X2V8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-208aa |
| 氨基酸序列 | MIRYCLTSYREDLVILDIINDSFSIVPDAGSLLKERDKLLKEFPQLSYFFDSEYHIGSVSRNSDTSFLEERWFLPEPDKTLYKCSLFKRFILLLKVFYYSWNIEKKGMAWIFISNKKENRLYSLNEEHLIRKEISNLSIIFHLNIFKSDCLTYSYALKRILNSRNIDAHLVIGVRTQPFYSHSWVEVGGQVINDAPNMRDKLSVIAEI |
| 预测分子量 | 32.0 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mcjB重组蛋白的模拟参考文献示例(注：由于该蛋白研究可能较为小众，以下内容为学术结构示例，建议结合具体研究领域核实真实文献)：
1. **标题**: *Cloning and Expression of Recombinant mcjB Protein in E. coli*
**作者**: Smith A, et al.
**摘要**: 本研究成功克隆了来自革兰氏阳性菌的mcjB基因，并利用大肠杆菌表达系统实现重组蛋白的高效可溶性表达，通过亲和层析纯化获得高纯度蛋白，为后续功能研究奠定基础。
2. **标题**: *Functional Characterization of mcjB as a Putative Toxin-Antitoxin System Component*
**作者**: Zhang L, et al.
**摘要**: 通过体外重组mcjB蛋白实验，发现其与mcjA形成毒素-抗毒素复合物，调控细菌应激反应，可能参与细菌生物被膜形成及持留态维持。
3. **标题**: *Structural Analysis of Recombinant McjB Using X-ray Crystallography*
**作者**: Tanaka K, et al.
**摘要**: 解析了重组McjB蛋白的2.1Å晶体结构，揭示其具有典型的核酸酶折叠结构域，推测其通过靶向DNA修复通路发挥抑菌作用。
4. **标题**: *McjB Recombinant Protein Enhances Antibiotic Susceptibility in Multidrug-Resistant Pathogens*
**作者**: Wang Y, et al.
**摘要**: 实验证明重组McjB蛋白可破坏耐药菌外膜通透性，与β-内酰胺类抗生素联用显著降低最小抑菌浓度，提示其作为抗生素佐剂潜力。
**备注**：以上为模拟文献结构，实际研究中mcjB可能与特定菌种(如艰难梭菌)的移动遗传元件相关。建议结合具体物种或功能关键词(如"mcjB toxin"、"bacterial recombination")在PubMed或Web of Science进一步检索。
The McjB protein is a bacterial protein encoded by the *mcjB* gene, first identified in *Escherichia coli* as part of the *mcj* (motility and colanic acid synthesis) operon. This operon is involved in regulating bacterial motility, biofilm formation, and stress responses. McjB acts as an accessory secretion factor, interacting with McjA, a small toxin-like protein that inhibits ATP synthesis by targeting the F1Fo ATP synthase. Together, McjA and McjB form a type I toxin-antitoxin (TA) system, where McjA acts as the toxin and McjB as the antitoxin. Under normal conditions, McjB neutralizes McjA’s activity, but under stress, McjA is released, transiently reducing bacterial metabolism and enhancing survival in hostile environments.
Recombinant McjB protein is engineered for studies on bacterial physiology and antimicrobial strategies. Its production typically involves cloning the *mcjB* gene into expression vectors (e.g., pET or pGEX systems) followed by overexpression in *E. coli* hosts. Purification via affinity chromatography (e.g., His-tag or GST-tag) yields soluble, functional protein. Research on recombinant McjB focuses on its structural interactions with McjA, its regulatory role in bacterial energetics, and its potential as a target for disrupting bacterial persistence mechanisms. Additionally, McjB has garnered interest in synthetic biology for designing controllable toxin-antitoxin modules to engineer microbial behavior. Understanding McjB’s function provides insights into bacterial stress adaptation and could inform novel approaches to combat antibiotic tolerance or biofilm-associated infections.
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