| 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 | 1/100-1/200 | 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 phosphorylation site of threonine 380/382/383 (R-Y-S(p)-D-T(p)-T(p)-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(Phospho-Ser380/Thr382/Thr383)抗体的3篇参考文献示例(注：内容为模拟概括，非真实文献)：
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1. **文献名称**：*Phosphorylation of PTEN C-terminal tail regulates its stability and tumor suppressor function*
**作者**：Vazquez F, et al.
**摘要**：本研究阐明了PTEN C端尾部多个位点(包括Ser380、Thr382/Thr383)的磷酸化对其蛋白稳定性的调控作用。作者通过制备特异性磷酸化抗体，证明这些位点的磷酸化抑制PTEN的泛素化降解，并影响其膜定位和脂质磷酸酶活性，进而调控肿瘤发生。
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2. **文献名称**：*AKT-mediated phosphorylation of PTEN at Ser380/Thr382/Thr383 modulates its interaction with PDZ domain proteins*
**作者**：Tibarewal P, et al.
**摘要**：研究利用磷酸化特异性抗体发现，AKT激酶介导的PTEN C端磷酸化(Ser380/Thr382/Thr383)会阻碍其与PDZ结构域蛋白的结合，从而改变PTEN的亚细胞分布和信号转导功能，揭示了磷酸化在PTEN蛋白互作中的关键作用。
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3. **文献名称**：*Development of a monoclonal antibody targeting PTEN phosphorylated at Ser380/Thr382/Thr383 for cancer diagnostics*
**作者**：Shi Y, et al.
**摘要**：本文报道了一种针对PTEN磷酸化位点(Ser380/Thr382/Thr383)的单克隆抗体的开发与验证。该抗体通过ELISA和免疫组化验证了特异性，并在多种癌症组织中检测到PTEN磷酸化水平的异常升高，提示其作为潜在生物标志物的价值。
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(注意：以上文献为示例性内容，实际引用需以真实发表的论文为准。)
The PTEN (Phospho-Ser380/Thr382/Thr383) antibody is a critical tool for studying the post-translational regulation of the PTEN tumor suppressor protein, a key negative regulator of the PI3K/AKT signaling pathway. PTEN acts as a lipid phosphatase, converting PIP3 to PIP2 to inhibit cell proliferation, survival, and growth. Its activity is tightly controlled by phosphorylation, particularly at the C-terminal cluster (Ser380. Thr382. Thr383. and Ser385). Phosphorylation at Ser380/Thr382/Thr383 induces a closed conformation, reducing PTEN’s membrane affinity and enzymatic activity while enhancing protein stability. This modification is mediated by kinases such as CK2 and GSK-3β and is reversed by PP2A phosphatases.
The PTEN (Phospho-Ser380/Thr382/Thr383) antibody specifically detects these phosphorylation sites, enabling researchers to investigate PTEN inactivation mechanisms in diseases like cancer, where dysregulated PTEN contributes to hyperactivated PI3K/AKT signaling. It is widely used in techniques including Western blotting, immunohistochemistry, and immunofluorescence to assess phosphorylation status in cell lines, tissues, or preclinical models. Studies utilizing this antibody have clarified how PTEN phosphorylation impacts cellular localization, protein-protein interactions, and tumor suppressor function, offering insights into therapeutic strategies targeting PTEN-related pathways. Proper controls, such as phosphorylation-deficient mutants, are essential to confirm antibody specificity.
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