| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DCUN1D1 |
| Uniprot No | Q96GG9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-259aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMNKLKSSQKDKVRQFMIFTQSSEKTAVSCL SQNDWKLDVATDNFFQNPELYIRESVKGSLDRKKLEQLYNRYKDPQDENK IGIDGIQQFCDDLALDPASISVLIIAWKFRAATQCEFSKQEFMDGMTELG CDSIEKLKAQIPKMEQELKEPGRFKDFYQFTFNFAKNPGQKGLDLEMAIA YWNLVLNGRFKFLDLWNKFLLEHHKRSIPKDTWNLLLDFSTMIADDMSNY DEEGAWPVLIDDFVEFARPQIAGTKSTTV |
| 预测分子量 | 32 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DCUN1D1重组蛋白的3篇参考文献概览：
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1. **文献名称**：*Structural basis for the role of DCUN1D1 in the neddylation pathway*
**作者**：Scott, D.C. et al.
**摘要**：本研究通过X射线晶体学解析了重组DCUN1D1蛋白的3D结构，揭示了其与Cullin蛋白及UBE2M泛素结合酶的相互作用位点，阐明了DCUN1D1在蛋白质neddylation(类泛素化修饰)中的支架功能，为靶向癌症治疗提供结构基础。
2. **文献名称**：*DCUN1D1 is a novel component of the NEDD8 conjugation pathway critical for cell proliferation*
**作者**：Kurz, T. et al.
**摘要**：通过体外重组蛋白实验，证明DCUN1D1直接参与Cullin家族蛋白的neddylation修饰，调控细胞周期进程。敲低DCUN1D1导致细胞增殖停滞，提示其作为癌基因在肿瘤发生中的潜在作用。
3. **文献名称**：*SCCRO (DCUN1D1) promotes nuclear translocation of NF-κB in lung cancer*
**作者**：Wu, K. et al.
**摘要**：利用重组DCUN1D1蛋白进行体外结合实验，发现其通过激活NF-κB信号通路促进肺癌细胞侵袭转移。研究进一步验证了DCUN1D1在肿瘤微环境中的促炎因子调控功能。
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**注**：DCUN1D1(又名SCCRO)是neddylation通路的关键调控因子，上述研究均通过重组蛋白技术解析其结构、互作网络或功能机制，相关成果对癌症靶向治疗研究具有重要参考价值。如需具体DOI或年份信息可进一步补充。
DCUN1D1 (Defective in Cullin Neddylation 1 Domain Containing 1) is a member of the DCN1 family of proteins involved in the regulation of protein neddylation, a post-translational modification closely related to ubiquitination. It plays a critical role in the activation of Cullin-RING E3 ubiquitin ligases (CRLs), which mediate the ubiquitination of substrate proteins destined for proteasomal degradation. Specifically, DCUN1D1 facilitates the transfer of NEDD8 (a ubiquitin-like protein) to Cullin proteins, a process essential for CRL complex assembly and function. Dysregulation of DCUN1D1 has been linked to cancer progression, particularly in squamous cell carcinomas, where its overexpression correlates with enhanced tumor growth, metastasis, and therapeutic resistance.
The recombinant DCUN1D1 protein is engineered for in vitro studies to dissect its structural and functional properties. It typically includes conserved domains such as the N-terminal ubiquitin-binding region and the C-terminal PONY (DCUN1 domain) responsible for substrate recognition and interaction with Cullin scaffolds. Recombinant versions are often expressed in bacterial or mammalian systems with affinity tags (e.g., His-tag) to enable purification and detection. Researchers utilize this protein to investigate neddylation mechanisms, screen for small-molecule inhibitors, or study protein-protein interactions in CRL-mediated pathways. Its application extends to developing targeted therapies, as inhibiting DCUN1D1 may disrupt oncogenic signaling in cancers reliant on hyperactive CRL activity. Structural studies using recombinant DCUN1D1 also aid in mapping binding interfaces for drug design.
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