| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DCUN1D3 |
| Uniprot No | Q8IWE4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-304aa |
| 氨基酸序列 | MGQCVTKCKNPSSTLGSKNGDREPSNKSHSRRGAGHREEQVPPCGKPGGDILVNGTKKAEAATEACQLPTSSGDAGRESKSNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT |
| 分子量 | 60.7 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DCUN1D3蛋白的模拟参考文献示例(实际文献需通过学术数据库检索)：
1. **"Structural and Functional Analysis of DCUN1D3 in the SCF Ubiquitin Ligase Complex"**
- 作者：Zhang L, et al.
- 摘要：研究通过X射线晶体学解析了DCUN1D3蛋白的结构，揭示了其作为SCF复合体调节因子的作用机制，重点探讨了其在泛素化修饰中对底物识别的贡献。
2. **"DCUN1D3 Promotes Genomic Stability via Regulating DNA Replication in Squamous Cell Carcinoma"**
- 作者：Wang Y, et al.
- 摘要：证明DCUN1D3通过调控DNA复制相关蛋白的稳定性维持基因组完整性，其缺失会导致癌细胞对放疗敏感性增加，提示其在肿瘤治疗中的潜在价值。
3. **"DCUN1D3 Deficiency Enhances Chemotherapy Sensitivity in Non-Small Cell Lung Cancer"**
- 作者：Chen R, et al.
- 摘要：发现DCUN1D3表达水平与肺癌化疗耐药性相关，其下调可通过抑制SCF复合体功能增强顺铂等药物的抗癌效果。
**提示**：以上为模拟内容，实际文献建议通过 **PubMed**、**Google Scholar** 或 **Web of Science** 搜索关键词“DCUN1D3”“SCF complex”“cancer”获取最新研究。
**Background of Recombinant Human DCUN1D3 Protein**
DCUN1D3 (Defective in Cullin Neddylation 1 Domain Containing 3), also known as DCNL3 or Squamous Cell Carcinoma-Related Oncogene 3 (SCCRO3), is a member of the DCUN1 protein family implicated in protein neddylation—a post-translational modification critical for regulating ubiquitin E3 ligase activity. This protein plays a role in the activation of Cullin-RING ligases (CRLs) by facilitating the transfer of NEDD8 (a ubiquitin-like protein) to cullin proteins, a process essential for substrate recognition and proteasomal degradation.
Structurally, DCUN1D3 contains a conserved DCUN1 domain that interacts with cullins and components of the neddylation pathway. Dysregulation of DCUN1D3 has been linked to cancer progression, particularly in squamous cell carcinomas, where its overexpression or mutations may drive genomic instability, uncontrolled proliferation, or metastasis. Studies suggest it may act as either an oncogene or tumor suppressor, depending on cellular context.
Recombinant human DCUN1D3 protein is produced using engineered expression systems (e.g., *E. coli* or mammalian cells) to enable functional studies. It serves as a vital tool for investigating neddylation mechanisms, CRL complex dynamics, and DCUN1D3's role in disease. Its applications include *in vitro* binding assays, enzymatic activity studies, and screening for therapeutic agents targeting neddylation in cancer and other pathologies. Research on recombinant DCUN1D3 continues to uncover its diagnostic and therapeutic potential.
×
