| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRAIP |
| Uniprot No | Q9BWF2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-469aa |
| 氨基酸序列 | MPIRALCTICSDFFDHSRDVAAIHCGHTFHLQCLIQWFETAPSRTCPQCRIQVGKRTIINKLFFDLAQEEENVLDAEFLKNELDNVRAQLSQKDKEKRDSQVIIDTLRDTLEERNATVVSLQQALGKAEMLCSTLKKQMKYLEQQQDETKQAQEEARRLRSKMKTMEQIELLLQSQRPEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKASGEVADKLRKDLFSSRSKLQTVYSELDQAKLELKSAQKDLQSADKEIMSLKKKLTMLQETLNLPPVASETVDRLVLESPAPVEVNLKLRRPSFRDDIDLNATFDVDTPPARPSSSQHGYYEKLCLEKSHSPIQDVPKKICKGPRKESQLSLGGQSCAGEPDEELVGAFPIFVRNAILGQKQPKRPRSESSCSKDVVRTGFDGLGGRTKFIQPTDTVMIRPLPVKPKTKVKQRVRVKTVPSLFQAKLDTFLWS |
| 预测分子量 | 58.8 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TRAIP重组蛋白的3篇参考文献示例(部分信息为模拟虚构，实际文献需通过学术数据库检索确认)：
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1. **文献名称**：*Structural insights into TRAIP ubiquitin ligase activity through recombinant protein crystallography*
**作者**：Sheng Y. et al. (2020)
**摘要**：本研究通过重组表达并纯化人源TRAIP蛋白，解析其晶体结构，揭示其RING结构域介导泛素化修饰的分子机制，为理解TRAIP在DNA损伤应答中的作用提供结构基础。
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2. **文献名称**：*TRAIP regulates replication fork stability via recombination-dependent restart pathways*
**作者**：Hoffmann S. et al. (2021)
**摘要**：利用重组TRAIP蛋白进行体外泛素化实验，证明其与PCNA和复制叉相关蛋白的相互作用，阐明TRAIP通过调控复制叉重塑维持基因组稳定的新机制。
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3. **文献名称**：*Targeting TRAIP-dependent ubiquitination as a therapeutic strategy in cancer*
**作者**：Liu X. et al. (2022)
**摘要**：通过重组TRAIP蛋白高通量筛选小分子抑制剂，发现化合物可阻断其泛素连接酶活性，显著抑制肿瘤细胞增殖，提示靶向TRAIP的潜在抗癌应用。
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**提示**：建议通过PubMed或Google Scholar检索最新文献，关键词可尝试：
`TRAIP recombinant protein structure`
`TRAIP ubiquitin ligase function`
`TRAIP DNA repair mechanism`
TRAIP (TRAF-interacting protein), also known as TRIP or RNF206. is a multifunctional protein implicated in critical cellular processes, including DNA damage response, genome stability maintenance, and cell cycle regulation. Initially identified as a binding partner of TNF receptor-associated factors (TRAFs), TRAIP gained attention for its role in immune signaling pathways. However, subsequent studies revealed its broader significance in nuclear processes, particularly during DNA replication stress and repair. Structurally, TRAIP contains an N-terminal RING domain (mediating E3 ubiquitin ligase activity), a central coiled-coil region (facilitating protein interactions), and a C-terminal nuclear localization signal.
A key function of TRAIP lies in resolving replication fork stalling. During DNA replication, TRAIP is recruited to stalled forks, where it promotes ubiquitination events essential for fork restart or collapse, thereby preventing genomic instability. Its interaction with PCNA (proliferating cell nuclear antigen) and components of the Fanconi anemia pathway further underscores its role in replication stress management. Additionally, TRAIP regulates the G1/S cell cycle checkpoint by modulating p53 activity and participates in ribosomal RNA processing.
Genetic studies link TRAIP mutations to human diseases. Biallelic loss-of-function mutations cause primordial dwarfism and microcephaly, highlighting its importance in embryonic development. Conversely, TRAIP overexpression is observed in certain cancers, suggesting context-dependent roles in tumorigenesis. Recent research also explores its potential as a therapeutic target, particularly in cancers with replication stress vulnerabilities. Despite progress, TRAIP's precise molecular mechanisms and tissue-specific functions remain active areas of investigation, bridging DNA repair biology with developmental disorders and cancer therapeutics.
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