| 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 | 1/100-1/500 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | P531; TP53B; TP53BP1; TRP53BP1; Tumor suppressor p53-binding protein 1; p53-binding protein 1 |
| Entrez GeneID | 7158; |
| 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 serine 25 (E-D-S(p)-Q-P) derived from Human 53BP1. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是3篇涉及53BP1(Phospho-Ser25)抗体的参考文献概要：
1. **"53BP1 phosphorylation on Ser25 regulates DNA damage-induced oligomerization"**
- 作者：Wang et al.
- 摘要：研究揭示了53BP1在Ser25位点的磷酸化对其在DNA双链断裂后形成功能性寡聚体的必要性，并验证了Phospho-Ser25抗体在检测损伤依赖性构象变化中的应用。
2. **"Cell cycle-dependent phosphorylation regulates 53BP1 pathway choice in DNA repair"**
- 作者：Botuyan et al.
- 摘要：通过Phospho-Ser25特异性抗体，作者证明细胞周期阶段通过调控Ser25磷酸化影响53BP1在非同源末端连接(NHEJ)与同源重组(HR)修复途径中的选择。
3. **"ATM-dependent phosphorylation of 53BP1 Ser25 modulates p53 activity in oxidative stress response"**
- 作者：Li et al.
- 摘要：研究发现ATM激酶依赖的Ser25磷酸化在氧化应激中调控53BP1与p53的相互作用，Phospho-Ser25抗体被用于验证该修饰在DNA损伤信号传导中的功能。
4. **"Phosphoproteomic analysis identifies 53BP1 Ser25 as a novel target in cancer radioresistance"**
- 作者：Zhang et al.
- 摘要：利用Phospho-Ser25抗体进行蛋白质组学筛选，揭示该位点磷酸化水平与肿瘤细胞放疗抗性相关，可能作为治疗靶点。
(注：上述文献为模拟示例，实际引用需查询具体数据库)
The 53BP1 (Phospho-Ser25) antibody detects a specific phosphorylation site (Ser25) on the 53BP1 protein, a key regulator of DNA damage response (DDR). 53BP1 (p53-binding protein 1) is involved in repairing DNA double-strand breaks (DSBs) by promoting non-homologous end joining (NHEJ). It localizes to sites of DNA damage through interactions with chromatin marks like H2A ubiquitination and H4K20 methylation. Phosphorylation at Ser25. mediated by kinases such as ATM/ATR during DDR, is critical for 53BP1’s recruitment to DSBs and its role in cell cycle checkpoint control. This modification may regulate 53BP1’s interactions with other repair proteins, influencing repair pathway choice (e.g., NHEJ vs. homologous recombination).
The 53BP1 (Phospho-Ser25) antibody is widely used in research to study DDR mechanisms, particularly in contexts like cancer therapy resistance, where 53BP1 dysfunction impacts genomic stability. It is validated for applications including Western blotting, immunofluorescence, and immunohistochemistry to assess phosphorylation-dependent 53BP1 activation. Studies using this antibody have elucidated how Ser25 phosphorylation affects 53BP1’s role in suppressing excessive DNA end resection, thereby preserving genome integrity. Its specificity makes it a valuable tool for exploring therapeutic strategies targeting DDR pathways in diseases like cancer.
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