| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTEN |
| Uniprot No | P60484 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-403aa |
| 氨基酸序列 | MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNI DDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLEL IKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQE ALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMF ETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVC GDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEI DSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKT VEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQI TKV |
| 预测分子量 | 48 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PTEN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 PTEN Tumor Suppressor: Implications for Its Phosphoinositide Phosphatase Activity and Membrane Association"**
**作者**：Lee, J.O., Yang, H., Georgescu, M.M., et al.
**摘要**：该研究通过X射线晶体学解析了重组人源PTEN蛋白的晶体结构，揭示了其催化结构域和C2结构域的构象，阐明了PTEN通过特异性水解PIP3(磷脂酰肌醇(3.4.5)-三磷酸)调控PI3K/AKT信号通路的分子机制，并探讨了其膜结合功能的结构基础。
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2. **文献名称**：**"Recombinant PTEN phosphatase: Purification and kinetic analysis of a tumor suppressor lipid phosphatase"**
**作者**：Myers, M.P., Pass, I., Batty, I.H., et al.
**摘要**：本文报道了利用杆状病毒-昆虫细胞系统表达重组PTEN蛋白的纯化方法，并对其磷酸酶活性进行了动力学分析。研究发现PTEN对PIP3的催化效率显著高于其他磷酸酶底物，且其活性受C端结构域调控，为后续靶向PTEN的功能研究提供了实验模型。
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3. **文献名称**：**"Structural basis for the inactivation of PTEN by phosphorylation-induced oligomerization"**
**作者**：Rahdar, M., Inoue, T., Meyer, T., et al.
**摘要**：研究通过重组PTEN蛋白的体外实验证明，其C端尾部的磷酸化会导致PTEN形成寡聚体，从而抑制其脂质磷酸酶活性。该机制解释了PTEN在细胞内的自抑制现象，为癌症中PTEN失活的分子机制提供了新见解。
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4. **文献名称**：**"Production of functional recombinant human PTEN protein in Escherichia coli: A tool for structural and functional studies"**
**作者**：Campbell, R.B., Liu, F., Ross, A.H.
**摘要**：该文献开发了一种在大肠杆菌中高效表达可溶性重组人PTEN蛋白的方法，并通过体外酶活实验验证了重组蛋白的功能活性。此方法为大规模制备PTEN蛋白用于药物筛选及结构生物学研究奠定了基础。
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以上文献涵盖了PTEN重组蛋白的结构解析、活性调控、制备方法等方向，均为该领域的重要研究。
PTEN (Phosphatase and tensin homolog) is a critical tumor suppressor protein encoded by the *PTEN* gene, widely recognized for its role in regulating cell growth, survival, and metabolic processes. Functioning primarily as a lipid phosphatase, it dephosphorylates phosphatidylinositol (3.4.5)-trisphosphate (PIP3), a key secondary messenger in the PI3K/AKT/mTOR signaling pathway. By antagonizing PI3K activity, PTEN helps maintain cellular homeostasis and prevents uncontrolled proliferation, making its loss or mutation a hallmark of numerous cancers, neurodevelopmental disorders, and metabolic diseases.
Recombinant PTEN proteins are engineered in vitro using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, functional PTEN for research and therapeutic applications. These proteins retain enzymatic activity and structural features of native PTEN, enabling studies on its molecular mechanisms, interactions with binding partners (e.g., membranes, regulatory proteins), and responses to post-translational modifications (e.g., phosphorylation, ubiquitination). Recombinant PTEN is also used to screen for inhibitors or activators that could modulate its activity in disease contexts.
Challenges in producing PTEN recombinantly include maintaining its solubility and stability, as the protein is prone to aggregation and degradation. Advanced purification techniques (e.g., affinity tags, chromatography) and optimized expression conditions are often employed to address these issues. Additionally, engineered variants (e.g., truncations, point mutations) help dissect PTEN's dual-specificity phosphatase functions or mimic pathological mutations observed in cancer.
Overall, recombinant PTEN serves as a vital tool for unraveling its biological roles, developing targeted therapies, and exploring its potential in regenerative medicine or precision oncology.
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