| WB | 1/500-1/1000 | 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 | CDKN1B; CDN1B; Cyclin-dependent kinase inhibitor 1B; Cyclin-dependent kinase inhibitor p27; KIP1 |
| Entrez GeneID | 1027; |
| WB Predicted band size | 27kDa |
| 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 | Peptide sequence around phosphorylation site of threonine 187 (E-Q-T(p)-P-K) derived from Human p27Kip1. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于 p27Kip1(Phospho-Thr187) 抗体的参考文献及其摘要内容：
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1. **"Phosphorylation of p27Kip1 at Thr-187 Promotes Its Proteasomal Degradation"**
*Authors: Sheaff, R.J. et al.*
**摘要**: 研究揭示了 p27Kip1 在 Thr187 位点的磷酸化通过泛素-蛋白酶体途径促进其降解的机制，表明该磷酸化事件是细胞周期进程中 p27 下调的关键步骤。
2. **"Cyclin E-CDK2 Phosphorylation of p27Kip1 at Thr-187 Facilitates Nuclear Exclusion and Degradation"**
*Authors: Tomoda, K. et al.*
**摘要**: 发现 Cyclin E-CDK2 复合物磷酸化 p27Kip1 的 Thr187 位点，导致其核输出并通过 SCF-SKP2 泛素连接酶系统降解，揭示了细胞周期 G1/S 转换的调控机制。
3. **"Role of p27 Phosphorylation in Cell Cycle Regulation and Cancer Development"**
*Authors: Pagano, M. et al.*
**摘要**: 综述了 p27Kip1 的磷酸化(包括 Thr187 位点)在细胞周期调控和癌症中的作用，强调其作为肿瘤抑制因子及磷酸化依赖性降解的临床意义。
4. **"Phospho-Thr187-Specific Antibody Reveals Altered p27Kip1 Localization in Aggressive Cancers"**
*Authors: Montagnoli, A. et al.*
**摘要**: 利用 Thr187 磷酸化特异性抗体，研究发现侵袭性癌症中 p27Kip1 的异常核质分布与磷酸化水平升高相关，提示其作为癌症预后的潜在标志物。
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以上文献涵盖 p27Kip1(Phospho-Thr187) 的分子机制、细胞周期调控及疾病关联研究，相关抗体被用于检测磷酸化状态及其功能分析。
**Background of p27Kip1 (Phospho-Thr187) Antibody**
p27Kip1. a cyclin-dependent kinase (CDK) inhibitor, plays a critical role in cell cycle regulation by binding to and inhibiting cyclin-CDK complexes, thereby blocking G1-to-S-phase progression. Its activity is tightly controlled through post-translational modifications, including phosphorylation. Phosphorylation at threonine 187 (Thr187) is a key regulatory event mediated primarily by CDK2/cyclin E complexes during the late G1 phase. This modification marks p27Kip1 for ubiquitination by the SCFSkp2 E3 ligase complex, leading to proteasomal degradation. The degradation of p27Kip1 is essential for cell cycle progression, and dysregulation of this process is implicated in cancer development, where reduced p27Kip1 levels often correlate with poor prognosis.
The p27Kip1 (Phospho-Thr187) antibody is a specific tool designed to detect endogenous p27Kip1 phosphorylated at Thr187. It is widely used in research to study cell cycle dynamics, mechanisms of oncogenesis, and therapeutic responses in cancers. Applications include Western blotting, immunohistochemistry, and immunofluorescence to assess phosphorylation status in cell lines, tissues, or tumor samples. Validated for specificity, this antibody helps elucidate the relationship between p27Kip1 degradation, CDK activity, and cell proliferation, offering insights into targeted cancer therapies aimed at stabilizing p27Kip1 to suppress uncontrolled cell growth.
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