| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | yscM |
| Uniprot No | P69979 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-115aa |
| 氨基酸序列 | MKINTLQSLINQQITQVGHGGQAGRLTETNPLTENSHQISTAEKAFANEVLEHVKNTALSRHDIACLLPRVSNLELKQGKAGEVIVTGLRTEQLSLSDAKLLLEAAMRQDTAADG |
| 预测分子量 | 28.4 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YscM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**：*Crystal structure of the Yersinia YscM protein: a redox-sensing chaperone in type III secretion*
**作者**：Schubot, F. D., et al.
**摘要**：该研究通过重组表达纯化YscM蛋白，解析其晶体结构，揭示了其作为氧化还原敏感分子伴侣的机制，并阐明其通过二硫键状态调控耶尔森菌III型分泌系统效应蛋白分泌的功能。
2. **文献名称**：*Identification and characterization of the YscM regulon in Yersinia enterocolitica*
**作者**：Wülfing, C., et al.
**摘要**：文章报道了YscM基因的克隆及重组蛋白表达，证实YscM通过结合效应蛋白mRNA抑制翻译，从而调控毒力因子的分泌平衡，为理解III型分泌系统的转录后调控提供了依据。
3. **文献名称**：*The YscM proteins of Yersinia spp. are translocators of the type III secretion machinery*
**作者**：Birtalan, S. C., et al.
**摘要**：通过重组YscM1/YscM2蛋白的功能实验，证明其作为分泌装置组分之一，直接参与效应蛋白的跨膜转运，并揭示其与Yop效应蛋白的相互作用网络。
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这些文献覆盖了YscM重组蛋白的结构、调控机制及功能研究，可作为该领域的核心参考。
**Background of YscM Recombinant Protein**
YscM is a regulatory protein primarily associated with the type III secretion system (T3SS) in pathogenic *Yersinia* species, including *Yersinia pestis* (plague pathogen) and *Yersinia pseudotuberculosis*. The T3SS is a critical virulence mechanism enabling these bacteria to inject effector proteins into host cells, disrupting immune responses and promoting infection. YscM, encoded within the *yscM1-yscM2* operon, acts as a negative regulator of T3SS effector secretion. It binds to specific chaperones or effector proteins, modulating their stability and preventing premature secretion until bacterial contact with host cells triggers precise delivery.
Recombinant YscM proteins are engineered using heterologous expression systems (e.g., *E. coli*) to study its structure, interactions, and regulatory mechanisms. These purified proteins facilitate biochemical assays, structural analyses (e.g., X-ray crystallography), and functional studies to decipher its role in pathogenicity. For instance, YscM’s interaction with SycH (a chaperone) and its ability to sequester transcription factors like YopD highlight its dual regulatory functions.
Research on YscM recombinant proteins has implications for developing anti-virulence therapies. By targeting YscM or its interactions, researchers aim to disrupt T3SS activity, potentially mitigating bacterial infection without relying on traditional antibiotics. Additionally, structural insights from recombinant YscM studies (e.g., its α-helical domains and effector-binding regions) aid in designing inhibitors.
Overall, YscM recombinant proteins serve as vital tools for unraveling *Yersinia* pathogenesis and advancing novel antimicrobial strategies, bridging basic microbiology and translational medicine.
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