| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | yopB |
| Uniprot No | P37131 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-401aa |
| 氨基酸序列 | MSALITHDRSTPVTGSLVPYIETPAPAPLQTQQVAGELKDKNGGVSSQGVQLPAPLAVVASQVTEGQQQEITKLLESVTRGTAGSQLISNYVSVLTNFTLASPDTFEIELGKLVSNLEEVRKDIKIADIQRLHEQNMKKIEENQEKIKETEENAKQVKKSGMASKIFGWLIAIASVVIGAIMVASGVGAVAGAMMIASGVIGMANMAVKQAAEDGLISQEAMQVLGPILTAIEVALTVVSTVMTFGGSALKCLADIGAKLGANTASLAAKGAEFSAKVAQISTGISNTVGSAVTKLGGSFGSLTMSHVIRTGSQATQVAVGVGSGITQTINNKKQADLQHNNADLALNKADMAALQSIIDRLKEELSHLSESHRQVMELIFQMINAKGDMLHNLAGRPHTV |
| 预测分子量 | 41,9 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YopB重组蛋白的3篇代表性文献的示例(内容基于典型研究，具体引用请核实原始文献)：
1. **文献名称**: *"YopB of Yersinia enterocolitica is essential for the translocation of Yop effector proteins into the cytosol of eukaryotic cells"*
**作者**: Hakansson, S., et al.
**摘要**: 研究证实YopB是鼠疫耶尔森菌III型分泌系统的关键蛋白，重组YopB在体外实验中显示其参与形成跨宿主细胞膜的孔道结构，促进其他效应蛋白的胞内递送。
2. **文献名称**: *"Role of YopB and YopD in the immune response to Yersinia infection"*
**作者**: Neyt, C., & Cornelis, G.R.
**摘要**: 通过重组YopB/YopD蛋白的免疫印迹分析，发现二者协同作用可抑制宿主巨噬细胞的吞噬功能，并调控促炎因子的释放，揭示了其在逃避免疫应答中的分子机制。
3. **文献名称**: *"Recombinant YopB expression in Escherichia coli and its role in pore formation"*
**作者**: Iriarte, M., & Cornelis, G.R.
**摘要**: 成功在大肠杆菌中表达并纯化重组YopB蛋白，证明其能在人工脂质体上形成孔道，进一步验证了YopB在破坏宿主细胞膜完整性中的直接作用。
**备注**：以上文献为示例，实际研究中请通过PubMed或Web of Science检索最新文献，并确保引用准确性。
YopB is a key virulence factor produced by pathogenic *Yersinia* species, including *Yersinia pestis* (plague bacterium) and *Yersinia enterocolitica*. It functions as a critical component of the type III secretion system (T3SS), a needle-like molecular syringe that injects bacterial effector proteins into host cells to suppress immune responses and promote infection. YopB, along with its partner protein YopD, forms a pore-like translocon complex in the host cell membrane, enabling the delivery of cytotoxic effectors like YopE and YopT. This pore formation disrupts cellular integrity and facilitates bacterial survival within the host.
Recombinant YopB refers to the protein produced via genetic engineering in heterologous expression systems (e.g., *E. coli*), allowing researchers to study its structure, function, and interactions in controlled settings. Studies on recombinant YopB have revealed its role in membrane interaction, particularly its ability to bind cholesterol and lipid rafts, which is crucial for translocon assembly. Its structural features, including hydrophobic domains and coiled-coil regions, are essential for pore formation and effector translocation.
Research on recombinant YopB has implications for understanding bacterial pathogenesis and developing therapeutics. For example, blocking YopB-mediated pore formation could neutralize *Yersinia* infections. Additionally, YopB’s immunogenic properties make it a candidate for vaccine development. Challenges in working with recombinant YopB include its tendency to aggregate due to hydrophobic regions, necessitating optimized purification strategies. Recent advances in structural biology, such as cryo-EM, have provided insights into YopB’s conformational dynamics within the T3SS, aiding drug design efforts. Overall, YopB remains a focal point in studying host-pathogen interactions and antibacterial strategies.
×
