| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pstP |
| Uniprot No | P9WHW4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-237aa |
| 氨基酸序列 | MARVTLVLRYAARSDRGLVRANNEDSVYAGARLLALADGMGGHAAGEVASQLVIAALAHLDDDEPGGDLLAKLDAAVRAGNSAIAAQVEMEPDLEGMGTTLTAILFAGNRLGLVHIGDSRGYLLRDGELTQITKDDTFVQTLVDEGRITPEEAHSHPQRSLIMRALTGHEVEPTLTMREARAGDRYLLCSDGLSDPVSDETILEALQIPEVAESAHRLIELALRGGGPDNVTVVVAD |
| 预测分子量 | 29.2 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PstP重组蛋白的3篇代表性文献示例(注：以下内容为模拟示例，实际文献请通过学术数据库查询)：
1. **文献名称**：Expression and Characterization of the Mycobacterium tuberculosis Serine/Threonine Phosphatase PstP
**作者**：Smith A, et al.
**摘要**：研究通过大肠杆菌系统成功表达并纯化重组PstP蛋白，证实其具有特异性Ser/Thr磷酸酶活性，并发现其活性依赖二价金属离子(如Mn²⁺)，为后续结核分枝杆菌信号通路研究提供工具。
2. **文献名称**：Structural Insights into PstP Phosphatase Reveal Potential Drug Target against Tuberculosis
**作者**：Chen L, et al.
**摘要**：通过X射线晶体学解析重组PstP蛋白的三维结构，揭示其催化机制关键位点，并通过抑制剂筛选实验验证其作为抗结核药物靶标的可行性。
3. **文献名称**：Functional Analysis of PstP in Mycobacterial Cell Wall Biosynthesis
**作者**：Kumar D, et al.
**摘要**：利用重组PstP蛋白进行体外磷酸化实验，证明其通过去磷酸化调控细胞壁合成相关激酶(PknB)的活性，进而影响分枝杆菌细胞壁稳态及抗生素耐受性。
---
**提示**：实际文献可通过PubMed或Google Scholar检索关键词 "PstP phosphatase recombinant Mycobacterium" 获取。部分经典文献可能来自《Journal of Biological Chemistry》《Molecular Microbiology》等期刊。
**Background of pstP Recombinant Protein**
The pstP (phosphoserine/threonine phosphatase) protein is a critical regulatory enzyme in bacterial signaling pathways, particularly in *Mycobacterium tuberculosis* and other actinobacteria. It belongs to the PPP (phosphoprotein phosphatase) family, which plays a central role in reversible protein phosphorylation, a key mechanism for regulating cellular processes. pstP specifically catalyzes the dephosphorylation of serine/threonine residues on target proteins, counterbalancing the activity of serine/threonine protein kinases (STPKs) to maintain metabolic homeostasis, stress adaptation, and virulence in pathogenic species.
Structurally, pstP contains a conserved catalytic domain with metal-binding motifs (e.g., Mn²⁺/Fe³⁺) essential for enzymatic activity, along with regulatory domains that modulate substrate specificity. In *M. tuberculosis*, pstP is implicated in controlling cell growth, division, and persistence by interacting with signaling components like the essential kinase PknB. Dysregulation of pstP activity has been linked to altered bacterial morphology, impaired biofilm formation, and reduced pathogenicity, highlighting its potential as a therapeutic target.
Recombinant pstP proteins are typically produced via heterologous expression in *E. coli* or other host systems. Cloning the *pstP* gene into expression vectors allows large-scale production, followed by purification using affinity chromatography. The recombinant protein retains enzymatic activity, enabling functional studies, inhibitor screening, and structural analysis (e.g., X-ray crystallography). Research on pstP has advanced understanding of bacterial signaling networks and informed drug discovery efforts targeting phosphatases to disrupt microbial viability.
Overall, pstP recombinant proteins serve as vital tools for exploring bacterial physiology and developing novel antimicrobial strategies.
×
