| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TP53BP1 |
| Uniprot No | Q12888 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3-4条关于TP53BP1重组蛋白的参考文献及其简要概括：
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1. **文献名称**：**"Structural basis of p53 recognition by 53BP1"**
**作者**：Derbyshire, D.J. et al.
**摘要**：该研究通过X射线晶体学解析了TP53BP1重组蛋白与p53肽段的复合物结构，揭示了其BRCT结构域与磷酸化p53的结合机制，阐明了其在DNA损伤应答中的分子基础。
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2. **文献名称**：**"Purification and functional analysis of recombinant 53BP1: A key mediator of DNA double-strand break repair"**
**作者**：Ward, I.M. et al.
**摘要**：报道了利用昆虫细胞系统表达并纯化重组TP53BP1蛋白，验证其在体外促进DNA损伤修复的功能，证明其通过招募下游修复因子(如RIF1)调控非同源末端连接(NHEJ)通路。
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3. **文献名称**：**"53BP1 regulates DNA resection and checkpoint activation in BRCA1-deficient cells"**
**作者**：Bunting, S.F. et al.
**摘要**：通过重组TP53BP1蛋白的生化实验，发现其通过抑制DNA末端切除酶活性调控同源重组修复缺陷细胞的基因组稳定性，为BRCA突变型癌症的治疗策略提供了理论依据。
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4. **文献名称**：**"High-yield expression and characterization of 53BP1 Tudor domain for drug discovery"**
**作者**：Zhang, Y. et al.
**摘要**：开发了一种高效表达和纯化TP53BP1 Tudor结构域重组蛋白的方法，用于筛选靶向其甲基化识别功能的小分子抑制剂，为癌症治疗药物开发提供工具。
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以上文献涵盖结构解析、功能验证及药物开发应用，均涉及重组TP53BP1蛋白的实验研究。
TP53BP1 (tumor protein p53-binding protein 1) is a critical DNA damage response (DDR) protein involved in maintaining genomic stability. It was initially identified as a p53-interacting partner that enhances p53-mediated transcriptional activation, though its role extends beyond p53 regulation. Structurally, TP53BP1 contains several functional domains: an N-terminal GAR/BRCT domain for chromatin interaction, tandem Tudor domains that recognize histone H4K20 methylation (a marker of DNA damage), and a C-terminal UDR motif facilitating binding to ubiquitinated substrates. These features enable TP53BP1 to act as a chromatin sensor, recruiting downstream repair factors to sites of DNA double-strand breaks (DSBs).
In DDR, TP53BP1 primarily promotes non-homologous end joining (NHEJ) over homologous recombination (HR) by antagonizing BRCA1. thus influencing repair pathway choice. This function is vital in cells during G1 phase, where HR is inactive. Dysregulation of TP53BP1 is linked to genomic instability, cancer predisposition, and therapy resistance. For instance, TP53BP1 loss impairs class-switch recombination in B-cells and sensitizes cancer cells to PARP inhibitors in BRCA1-deficient backgrounds.
Recombinant TP53BP1 proteins are engineered for in vitro studies to dissect its molecular mechanisms, including phosphorylation-dependent interactions, chromatin binding, and repair complex assembly. These purified proteins are essential tools for structural analyses (e.g., crystallography), biochemical assays (ubiquitination, phosphorylation), and high-throughput drug screening. Therapeutic strategies targeting TP53BP1 are emerging, aiming to modulate DDR in cancer therapy or overcome treatment resistance. However, its dual roles in tumor suppression and therapy response necessitate careful evaluation in clinical applications.
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