| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DCUN1D5 |
| Uniprot No | Q9BTE7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-237aa |
| 氨基酸序列 | MPVKKKRKSPGVAAAVAEDGGLKKCKISSYCRSQPPARLISGEEHFSSKKCLAWFYEYAGPDEVVGPEGMEKFCEDIGVEPENIIMLVLAWKLEAESMGFFTKEEWLKGMTSLQCDCTEKLQNKFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTWPLFSVFYQYLEQSKYRVMNKDQWYNVLEFSRTVHADLSNYDEDGAWPVLLDEFVEWQKVRQTS |
| 分子量 | 53.9 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人DCUN1D5蛋白的示例参考文献(*注：文献名为模拟生成，仅供参考*)：
1. **"DCUN1D5 promotes lung cancer progression via stabilizing cullin 3 ubiquitin ligase"**
- 作者：Zhang L. et al.
- 摘要：研究利用重组人DCUN1D5蛋白揭示了其通过调控Cullin 3泛素连接酶的稳定性促进肺癌细胞增殖和迁移的分子机制。
2. **"Structural insights into DCUN1D5-SAG complex in neddylation pathway"**
- 作者：Wang Y. et al.
- 摘要：通过X射线晶体学解析重组DCUN1D5与SAG蛋白的复合物结构，阐明其在类泛素化(neddylation)通路中的关键作用。
3. **"DCUN1D5 enhances Wnt/β-catenin signaling by facilitating neddylation of E3 ligase components"**
- 作者：Chen H. et al.
- 摘要：重组DCUN1D5蛋白功能实验表明，其通过介导E3泛素连接酶的类泛素化修饰，正向调控Wnt/β-catenin信号通路，促进结直肠癌发展。
4. **"Knockdown of DCUN1D5 inhibits tumor growth via p53-dependent apoptosis"**
- 作者：Kim S. et al.
- 摘要：通过重组蛋白和基因沉默实验，发现DCUN1D5通过调控p53泛素化降解抑制肿瘤细胞凋亡，提示其作为潜在治疗靶点。
建议通过PubMed或Google Scholar搜索 **DCUN1D5 recombination protein** 或 **SCP-DCUN1D5(别名)** 获取真实文献。
Recombinant human DCUN1D5 protein is a genetically engineered form of the DCUN1D5 (Defective in Cullin Neddylation 1 Domain Containing 5) protein, which plays a critical role in regulating protein neddylation—a post-translational modification process essential for the activity of cullin-RING E3 ubiquitin ligases (CRLs). DCUN1D5. a member of the DCUN1 protein family, acts as a co-factor in the neddylation cascade by facilitating the transfer of NEDD8 (a ubiquitin-like protein) to cullin scaffolds. This modification is vital for CRL complex assembly, substrate ubiquitination, and subsequent proteasomal degradation of target proteins. Dysregulation of DCUN1D5 has been implicated in tumorigenesis, particularly in cancers linked to disrupted protein homeostasis, such as squamous cell carcinomas. The recombinant form, typically produced in *E. coli* or mammalian expression systems, enables functional studies on its interactions with cullins, NEDD8. and other regulatory components. Researchers utilize this protein to investigate mechanisms underlying DNA repair, cell cycle control, and Wnt/β-catenin signaling, where CRLs are key players. Its recombinant availability also supports drug discovery efforts targeting neddylation pathways for cancer therapy. Structural and biochemical analyses of recombinant DCUN1D5 provide insights into its UBA-like domain functionality and potential mutations affecting disease progression.
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