| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | yopH |
| Uniprot No | Q3UND0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-358aa |
| 氨基酸序列 | MPNPSCTSSP GPLPEEIRNL LADVETFVAD TLKGENLSKK AKEKRESLIK KIKDVKSVYL QEFQDKGDAE DGDEYDDPFA GPADTISLAS ERYDKDDDGP SDGNQFPPIA AQDLPFVIKA GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIDGYD VRMNNTLRKD GKKDCCFEIC APDKRIYQFT AASPKDAEEW VQQLKFILQD LGSDVIPEDD EERGELYDDV DHPAAVSSPQ RSQPIDDEIY EELPEEEEDT ASVKMDEQGK GSRDSVHHTS GDKSTDYANF YQGLWDCTGA LSDELSFKRG DVIYILSKEY NRYGWWVGEM KGAIGLVPKA YLMEMYDI |
| 预测分子量 | 40,7 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YopH重组蛋白的3篇参考文献及摘要概括：
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1. **文献名称**: *Purification and characterization of recombinant Yersinia protein tyrosine phosphatase (YopH)*
**作者**: Zhang, Z.Y., et al.
**摘要**: 该研究通过大肠杆菌表达系统成功制备了重组YopH蛋白，并对其酪氨酸磷酸酶活性进行了表征。结果显示，YopH对含磷酸酪氨酸的宿主蛋白具有高效去磷酸化作用，提示其在耶尔森氏菌逃避宿主免疫中的作用。
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2. **文献名称**: *Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å resolution*
**作者**: Stuckey, J.A., et al.
**摘要**: 通过X射线晶体学解析了YopH的三维结构，揭示了其催化活性中心的关键氨基酸残基及底物结合模式，为开发针对耶尔森氏菌感染的抑制剂提供了结构基础。
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3. **文献名称**: *YopH of Yersinia pseudotuberculosis interrupts phagocytic signaling through inactivation of focal adhesion kinase in macrophages*
**作者**: Persson, C., et al.
**摘要**: 研究证明重组YopH通过特异性去磷酸化宿主细胞黏着斑激酶(FAK)，抑制巨噬细胞的吞噬功能，进一步阐明了其在细菌致病性中的分子机制。
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如需更多文献或具体细节，可提供进一步研究方向。
YopH, a key virulence factor of *Yersinia pestis* (the causative agent of plague), is a tyrosine phosphatase secreted via the type III secretion system (T3SS) during infection. It plays a critical role in subverting host immune defenses by disrupting intracellular signaling pathways in phagocytes. YopH targets phosphorylated tyrosine residues on host proteins, effectively deactivating signaling molecules involved in phagocytosis, cytokine production, and oxidative burst responses. This enzymatic activity allows *Yersinia* to evade immune detection and establish systemic infection.
The recombinant YopH protein, often expressed in *E. coli* systems for research purposes, retains the functional phosphatase domain and is widely used to study bacterial pathogenesis and host-pathogen interactions. Its structure includes an N-terminal secretion signal and a C-terminal catalytic domain, with the latter sharing homology with eukaryotic phosphatases, making it a model for studying phosphatase mechanisms. Research on YopH has provided insights into immune evasion strategies, potential therapeutic targets, and the development of inhibitors to counteract its activity.
Additionally, YopH’s role in disrupting focal adhesion complexes and T-cell receptor signaling has expanded its relevance to broader studies in immunology and cell biology. Its recombinant form enables in vitro assays, structural studies (e.g., X-ray crystallography), and screening platforms for antimicrobial agents. Understanding YopH’s function not only advances plague research but also contributes to knowledge of bacterial effector proteins and their manipulation of host systems.
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