| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/100-1/500 | 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 | Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1, CDKN1B, KIP1 |
| Entrez GeneID | 1027 |
| WB Predicted band size | 22.1kDa |
| 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 p27Kip1 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding T187 of human p27Kip1. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是3篇与Phospho-p27Kip1(T187)抗体相关的经典文献摘要：
1. **文献名称**：*Phosphorylation of p27Kip1 on Thr187 by Cyclin E/Cdk2 Modulates Its Stability*
**作者**：Sheaff, R.J. 等(1997)
**摘要**：首次阐明p27在Thr187位点被Cyclin E/Cdk2磷酸化是触发其通过泛素-蛋白酶体途径降解的关键步骤，揭示了该磷酸化事件与细胞周期G1/S期转换的关联。
2. **文献名称**：*Ubiquitination of p27Kip1 by SCF-Skp2 Complex*
**作者**：Pagano, M. 等(1997)
**摘要**：证明SCF-Skp2泛素连接酶特异性识别并降解Thr187磷酸化的p27.阐明了磷酸化p27在肿瘤中低表达的机制，为癌症治疗提供靶点。
3. **文献名称**：*Phosphorylation-Dependent Degradation of p27 via Nuclear Export in Cancer*
**作者**：Tomoda, K. 等(1999)
**摘要**：发现磷酸化的p27通过CRM1依赖性核输出途径被转运至胞质降解，解释了其在恶性肿瘤细胞中异常定位与功能失调的关联。
4. **文献名称**：*Regulation of p27Kip1 Phosphorylation and Cellular Localization*
**作者**：Slingerland, J. & Polyak, K. (综述，1997)
**摘要**：系统总结了p27的磷酸化(包括T187位点)对其稳定性、亚细胞定位及细胞周期调控的影响，强调其在肿瘤发生中的双重作用。
这些文献聚焦于T187磷酸化如何调控p27的稳定性、降解机制及其在癌症中的病理意义，为使用该抗体的功能研究提供理论依据。
Phospho-p27Kip1 (Thr187) antibody is a specialized tool used to detect the phosphorylated form of the p27Kip1 protein at threonine residue 187. p27Kip1. encoded by the CDKN1B gene, is a cyclin-dependent kinase (CDK) inhibitor that regulates cell cycle progression by binding to and inhibiting cyclin-CDK complexes, particularly during the G1-to-S phase transition. Phosphorylation at Thr187 is a critical post-translational modification that marks p27Kip1 for proteasomal degradation. This phosphorylation event is mediated by cyclin E-CDK2 complexes during the late G1 phase, promoting S-phase entry by reducing p27Kip1 levels.
The Phospho-p27Kip1 (Thr187) antibody is widely used in cancer research, as dysregulation of p27Kip1 degradation is linked to tumor progression and poor prognosis. Elevated phosphorylation at Thr187 correlates with increased cell proliferation, aggressive tumor behavior, and resistance to therapies in various cancers. Researchers employ this antibody in techniques like Western blotting, immunohistochemistry, and flow cytometry to assess p27Kip1 phosphorylation status in cell lines, tissues, or clinical samples. Its specificity for the phosphorylated epitope allows differentiation between active (phosphorylated) and inactive forms, providing insights into cell cycle dynamics, therapeutic responses, and mechanisms of oncogenesis. Validation using appropriate controls (e.g., phosphorylation-blocking peptides) is essential to ensure antibody specificity.
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