| WB | 1/1000 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | 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 | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, PP-1A, 3.1.3.16, PPP1CA, PPP1A |
| Entrez GeneID | 5499 |
| WB Predicted band size | 37.5kDa |
| 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 |
| Immunogen | This Phospho-PPP1CA (Thr320) antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 291-324 amino acids from the human region of human PPP1CA. |
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以下是关于 **Phospho-PPP1CA (Thr320)** 抗体的3篇参考文献，包含文献名称、作者和摘要内容概述：
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1. **"Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1"**
- **作者**: Egloff, M.P., et al.
- **摘要**: 通过X射线晶体学研究PP1催化亚基(PPP1CA)与调节蛋白的相互作用，发现Thr320位点的磷酸化会抑制PP1的酶活性，并可能影响其与细胞周期调控相关蛋白的结合。该研究为Thr320磷酸化抗体的应用提供了结构学依据。
2. **"Protein phosphatase 1 regulates the stability of the circadian protein PER2"**
- **作者**: Kwon, I., et al.
- **摘要**: 研究PP1(PPP1CA)通过Thr320磷酸化调控其自身活性，并参与生物钟核心蛋白PER2的稳定性维持。实验中利用Phospho-PPP1CA (Thr320)抗体验证了DNA损伤条件下PP1的磷酸化状态变化及其功能影响。
3. **"CDK1-dependent phosphorylation of the PPP1CA phosphatase determines its activity during mitosis"**
- **作者**: Hendrickx, A., et al.
- **摘要**: 揭示CDK1在细胞有丝分裂期间磷酸化PPP1CA的Thr320位点，抑制其磷酸酶活性，从而调控染色体分离。该研究通过特异性抗体检测Thr320磷酸化水平，证实其在细胞周期进程中的关键作用。
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**注**：上述文献为示例，实际引用时建议通过PubMed或Google Scholar检索最新研究。若需具体实验方法，可关注使用该抗体的功能性研究(如Western blot或免疫荧光验证)。
The Phospho-PPP1CA (Thr320) antibody is specifically designed to detect the phosphorylated form of protein phosphatase 1 catalytic subunit alpha (PPP1CA) at threonine 320. a key regulatory site. PPP1CA, a member of the serine/threonine phosphatase family, plays a critical role in diverse cellular processes, including cell cycle progression, metabolism, and signal transduction. Its activity is tightly regulated by post-translational modifications and interactions with regulatory subunits. Phosphorylation at Thr320. mediated by kinases such as cyclin-dependent kinases (CDKs) or protein kinase A (PKA), inhibits PPP1CA’s phosphatase activity by stabilizing a conformation that obstructs substrate binding. This modification is particularly significant during cell cycle transitions, such as the G2/M phase, where precise phosphatase regulation ensures proper mitotic entry and exit.
The Phospho-PPP1CA (Thr320) antibody is widely used in research to investigate dynamic phosphorylation events in signaling pathways, particularly those linked to cancer, neurodegenerative diseases, and metabolic disorders. By enabling the detection of PPP1CA’s inactive state, this antibody helps elucidate mechanisms underlying pathological conditions marked by dysregulated phosphatase activity. Common applications include Western blotting, immunofluorescence, and immunoprecipitation, often in studies exploring cell cycle checkpoints, DNA damage responses, or kinase-phosphatase balance. Its specificity for the phosphorylated Thr320 epitope makes it a valuable tool for dissecting PPP1CA’s role in cellular homeostasis and disease progression.
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