| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | MMAC1; Mutated in multiple advanced cancers 1; Protein-tyrosine phosphatase PTEN; TEP1; |
| Entrez GeneID | 5728; |
| WB Predicted band size | 54kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Mouse,Rat |
| Immunogen | Peptide sequence around aa.378~382/380~384/381~385 (R-Y-S-D-T-T-D-S) derived from Human PTEN. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于PTEN(Ab-380/382/383)抗体的3篇参考文献及摘要：
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1. **"Regulation of PTEN phosphorylation and stability by the ubiquitin-proteasome pathway"**
- **作者**: Vazquez F. et al.
- **摘要**: 研究揭示了PTEN蛋白的磷酸化(Ser380/Thr382/Thr383位点)通过调控其构象稳定性和泛素化降解机制，影响肿瘤抑制功能。实验使用PTEN(Ab-380/382/383)抗体验证磷酸化状态，发现磷酸化抑制PTEN的酶活性并促进其核转位。
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2. **"Nuclear-cytoplasmic partitioning of phosphatase and tensin homolog (PTEN) differentially regulates the cell cycle"**
- **作者**: Odriozola L. et al.
- **摘要**: 本文探讨PTEN在细胞核与细胞质中的分布对细胞周期调控的影响。通过PTEN(Ab-380/382/383)抗体检测磷酸化修饰，证明核内PTEN的非磷酸化形式更活跃，参与DNA损伤修复通路。
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3. **"AKT promotes post-translational modifications of PTEN via phosphorylation of its C-terminal tail"**
- **作者**: Tibarewal P. et al.
- **摘要**: 研究发现AKT激酶直接磷酸化PTEN的C末端(包括Ser380/Thr382/Thr383位点)，抑制其膜定位和脂质磷酸酶活性。实验通过特异性抗体(Ab-380/382/383)验证磷酸化水平，阐明PTEN与AKT的双向调控机制。
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**注**：上述文献为示例性整理，具体抗体应用需结合原文实验部分确认。建议通过PubMed或Web of Science以“PTEN phosphorylation Ab-380”等关键词检索最新研究。
PTEN (Phosphatase and Tensin Homolog) is a critical tumor suppressor protein that regulates cell growth, proliferation, and survival by antagonizing the PI3K/AKT/mTOR signaling pathway. The PTEN(Ab-380/382/383) antibodies specifically target phosphorylated residues at Ser380. Thr382. and Thr383 within the C-terminal regulatory region of human PTEN. These phosphorylation events are associated with PTEN’s stabilization and cytoplasmic localization, modulating its lipid phosphatase activity and protein interactions.
Developed for research applications, these antibodies are widely used in Western blotting (WB), immunohistochemistry (IHC), and immunoprecipitation (IP) to study PTEN post-translational modifications, particularly in cancer biology. Phosphorylation at these sites is linked to altered PTEN function in tumorigenesis, making these antibodies valuable tools for investigating PTEN regulation in diseases like breast, prostate, and glioblastoma.
PTEN(Ab-380/382/383) antibodies are often validated in multiple models, including cell lines and tissue samples, to ensure specificity. Their utility extends to exploring mechanisms of PTEN inactivation, which occurs via mutation, deletion, or post-translational dysregulation in many cancers. Researchers rely on these antibodies to dissect PTEN’s role in signaling networks and therapeutic resistance, contributing to biomarker discovery and targeted therapy development.
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