| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTRH2 |
| Uniprot No | Q9Y3E5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 64-179aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMEYKMILVVRNDLKMGKGKVAAQCSHAAVS AYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSL IQDAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY |
| 预测分子量 | 15 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PTRH2重组蛋白的3篇代表性文献，信息基于公开研究领域知识整理，非真实文献：
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1. **文献名称**：*PTRH2重组蛋白的肿瘤抑制功能及机制研究*
**作者**：Xu et al.
**摘要**：本研究在大肠杆菌系统中成功表达并纯化了重组PTRH2蛋白，体外实验表明其通过调控线粒体凋亡通路抑制肿瘤细胞增殖，提示PTRH2可能作为新型抑癌蛋白发挥作用。
2. **文献名称**：*PTRH2重组蛋白的结构解析及其酶活性分析*
**作者**：Chen et al.
**摘要**：通过X射线晶体学解析了重组PTRH2蛋白的三维结构，揭示了其氨基端具有保守的肽酶活性位点，功能实验证实其参与应激条件下错误折叠蛋白的降解。
3. **文献名称**：*PTRH2重组蛋白在代谢综合征中的调控作用*
**作者**：Zhang et al.
**摘要**：在糖尿病模型中，重组PTRH2蛋白通过改善线粒体功能缓解胰岛素抵抗，机制涉及对mTOR信号通路的负向调控，为代谢疾病治疗提供了新靶点。
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**说明**：上述文献为领域知识模拟，实际引用需查询PubMed、Web of Science等数据库获取真实文献(例如搜索关键词：PTRH2 recombinant protein, PTRH2 structure/function)。
The PTRH2 (Peptidyl-tRNA Hydrolase 2) recombinant protein is derived from the human PTRH2 gene, located on chromosome 17q21.2. This gene encodes a mitochondrial protein with conserved peptidyl-tRNA hydrolase activity, essential for rescuing stalled translation machinery by hydrolyzing peptidyl-tRNA molecules. PTRH2 plays a critical role in maintaining mitochondrial proteostasis, energy metabolism, and cellular stress responses. Studies suggest its involvement in apoptosis regulation, mitochondrial dynamics, and DNA damage repair pathways, linking it to neurodegenerative disorders, cancer, and developmental defects.
Recombinant PTRH2 protein is typically produced using bacterial or mammalian expression systems, enabling large-scale purification for functional studies. Its recombinant form retains enzymatic activity, making it a valuable tool for in vitro assays to dissect molecular mechanisms of tRNA processing, mitochondrial dysfunction, or stress signaling. Structural studies using recombinant PTRH2 have revealed conserved catalytic residues and substrate-binding domains, offering insights into its evolutionary conservation across eukaryotes.
Clinically, PTRH2 mutations are associated with infantile-onset multisystem neurologic, endocrine, and pancreatic disease (IMNEPD), underscoring its importance in neurodevelopment. Recombinant protein-based models help investigate pathogenic mutations and test therapeutic interventions. Additionally, its role in tumor suppression (e.g., inhibiting epithelial-mesenchymal transition in cancers) has spurred interest in cancer research. The protein’s dual localization (mitochondrial and nuclear) further expands its research applications in cellular compartment-specific studies. Ongoing work aims to leverage recombinant PTRH2 for drug screening and biomarker development.
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