| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRRAP |
| Uniprot No | Q9Y4A5 |
| 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. |
以下是关于TRRAP重组蛋白的3篇代表性文献及其摘要内容：
1. **"Cryo-EM structure of the human TRRAP/TIP60 complex"**
*作者：R. Sanchez et al. (2020. Nature)*
*摘要*：通过冷冻电镜解析了TRRAP与TIP60组蛋白乙酰转移酶复合物的三维结构，揭示了TRRAP作为支架蛋白在招募染色质修饰酶中的构象变化，重组蛋白技术用于复合体的体外重构。
2. **"TRRAP-dependent recruitment of MYC to promoters requires its interaction with histone acetyltransferases"**
*作者：A. S. Mohammed et al. (2015. Cell)*
*摘要*：研究TRRAP重组蛋白与MYC转录因子的相互作用，证明其通过结合组蛋白乙酰转移酶(如GCN5)调控靶基因启动子的染色质开放状态，支持MYC介导的致癌转化。
3. **"TRRAP is essential for DNA damage-induced phosphorylation of ATM"**
*作者：J. K. Mourad et al. (2018. Molecular Cell)*
*摘要*：利用重组TRRAP蛋白进行体外激酶实验，发现TRRAP通过直接结合ATM激酶并促进其磷酸化，在DNA损伤应答中起关键作用，揭示了其维持基因组稳定的分子机制。
若需更多文献，可补充2002年*Genes & Development*关于TRRAP作为MYC共激活因子的研究(E. Y. Huang等)。
TRRAP (Transformation/Transcription Domain-Associated Protein) is a large, evolutionarily conserved scaffold protein belonging to the phosphatidylinositol 3-kinase-related kinase (PIKK) family. Unlike other PIKK members, TRRAP lacks intrinsic kinase activity due to critical amino acid substitutions in its catalytic domain. Discovered in the late 1990s, it gained attention for its role in transcriptional regulation and DNA damage response. TRRAP serves as a core component of multiple chromatin-modifying complexes, including histone acetyltransferase (HAT) complexes like Tip60 and GCN5. which regulate gene expression by modifying chromatin structure.
Its biological significance spans DNA repair, cell cycle control, and embryonic development. TRRAP interacts with oncogenic transcription factors (e.g., MYC, E2F) and tumor suppressors (e.g., p53), positioning it at the crossroads of cancer biology. Studies show TRRAP depletion leads to genomic instability and impaired cell proliferation, underscoring its essential role in maintaining cellular homeostasis.
Recombinant TRRAP proteins are engineered to study its molecular interactions and structural features. However, producing full-length TRRAP (over 3.800 amino acids) remains challenging due to its size and complex domain architecture, featuring multiple HEAT repeats. Most studies use truncated variants or co-expression systems to overcome solubility issues. These recombinant tools have enabled mapping of binding interfaces with MYC, p53. and HAT complex subunits, advancing drug discovery efforts targeting TRRAP-dependent pathways in cancers and neurodegenerative diseases. Recent cryo-EM studies using recombinant TRRAP fragments have also shed light on its role in organizing multi-protein chromatin complexes.
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