| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIP12 |
| Uniprot No | Q14669 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1881-1992aa |
| 氨基酸序列 | ECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQQSFHLS |
| 预测分子量 | 19.9 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TRIP12重组蛋白的3篇代表性文献摘要(注：内容基于公开研究综合，非真实文献)：
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1. **文献名称**: *TRIP12 functions as an E3 ubiquitin ligase in regulating p53 stability*
**作者**: Wang Y, et al.
**摘要**: 本研究揭示了TRIP12作为E3泛素连接酶，通过直接泛素化修饰p53蛋白并促进其蛋白酶体降解，从而在DNA损伤应答中调控细胞周期进程。实验显示TRIP12缺失会导致p53积累，增强细胞凋亡。
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2. **文献名称**: *TRIP12 promotes tumor progression via Notch signaling in colorectal cancer*
**作者**: Li H, et al.
**摘要**: 该研究证实TRIP12在结直肠癌中高表达，通过泛素化降解Notch通路抑制因子NUMB，激活Notch信号，促进肿瘤细胞增殖和转移。临床数据分析表明TRIP12表达与患者不良预后相关。
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3. **文献名称**: *Structural insights into TRIP12-mediated ubiquitination*
**作者**: Zhang R, et al.
**摘要**: 通过冷冻电镜解析了TRIP12重组蛋白与UBE2D2(E2酶)复合物的三维结构，揭示了其底物识别和催化泛素转移的分子机制，为靶向TRIP12的癌症治疗药物设计提供了结构基础。
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如需具体文献，建议通过PubMed或Google Scholar以“TRIP12 ubiquitin ligase”或“TRIP12 cancer”为关键词检索。
TRIP12 (Thyroid Hormone Receptor Interactor 12) is a multifunctional protein encoded by the TRIP12 gene, belonging to the HECT (Homologous to E6-AP C-Terminus) family of E3 ubiquitin ligases. It plays a critical role in regulating protein turnover through the ubiquitin-proteasome system by tagging specific substrates with ubiquitin for degradation. Structurally, TRIP12 contains several domains, including Armadillo (ARM) repeats that mediate protein-protein interactions and a catalytic HECT domain essential for its ligase activity.
Originally identified as a thyroid hormone receptor-interacting protein, TRIP12 has since been implicated in diverse cellular processes, such as DNA damage repair, cell cycle regulation, and chromatin remodeling. It interacts with key regulators like p53. USP7 (a deubiquitinating enzyme), and components of the DNA repair machinery, fine-tuning their stability and activity. Dysregulation of TRIP12 is linked to pathological conditions, particularly cancer. For instance, TRIP12 mutations or altered expression have been observed in cancers of the breast, lung, and liver, where it may act as an oncogene by destabilizing tumor suppressors or promoting genomic instability. Conversely, in some contexts, TRIP12 exhibits tumor-suppressive functions, highlighting its context-dependent roles.
Recombinant TRIP12 protein, produced via heterologous expression systems (e.g., Escherichia coli or mammalian cells), serves as a vital tool for studying its biochemical properties, substrate specificity, and interaction networks. Purified recombinant TRIP12 enables in vitro ubiquitination assays, structural studies (e.g., crystallography or cryo-EM), and high-throughput drug screening to identify potential inhibitors for cancer therapy. Its recombinant form also aids in elucidating post-translational modifications and regulatory mechanisms underlying its dual roles in tumorigenesis. Ongoing research continues to explore TRIP12's therapeutic potential as a biomarker or target in precision oncology.
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