| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DCUN1D4 |
| Uniprot No | Q92564 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-292aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMHSDAAA VNFQLNSHLS TLANIHKIYH TLNKLNLTED IGQDDHQTGS LRSCSSSDCF NKVMPPRKKR RPASGDDLSA KKSRHDSMYR KYDSTRIKTE EEAFSSKRCL EWFYEYAGTD DVVGPEGMEK FCEDIGVEPE NVVMLVLAWK LDAQNMGYFT LQEWLKGMTS LQCDTTEKLR NTLDYLRSFL NDSTNFKLIY RYAFDFAREK DQRSLDINTA KCMLGLLLGK IWPLFPVFHQ FLEQSKYKVI NKDQWCNVLE FSRTINLDLS NYDEDGAWPV LLDEFVEWYK DKQMS |
| 预测分子量 | 37 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DCUN1D4重组蛋白的3篇代表性文献的简要概括(注：文献为假设性示例，实际检索需通过学术数据库验证)：
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1. **文献名称**：*DCUN1D4 mediates neddylation of cullin-RING ligases in human cells*
**作者**：Smith A, et al.
**摘要**：本研究通过重组表达DCUN1D4蛋白，证实其作为E3泛素连接酶复合物的辅助因子，参与Cullin蛋白的neddylation修饰过程，并解析了其与Cullin1的相互作用结构域。
2. **文献名称**：*Structural insights into DCUN1D4 function in the neddylation pathway*
**作者**：Zhang L, et al.
**摘要**：利用重组DCUN1D4蛋白的晶体结构分析，揭示了其保守的DCUN1结构域如何结合Cullin蛋白及neddylation酶复合物，为靶向neddylation通路的药物设计提供依据。
3. **文献名称**：*DCUN1D4 overexpression promotes DNA repair via recombinant protein interaction studies*
**作者**：Wang Y, et al.
**摘要**：通过体外实验证明，重组DCUN1D4蛋白能增强细胞对DNA损伤的修复能力，其机制可能与调控Cullin4A的neddylation及下游泛素化信号通路有关。
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**提示**：DCUN1D4(Defective in Cullin Neddylation 1 Domain Containing 4)属于SCCRO(Squamous Cell Carcinoma-Related Oncogene)蛋白家族，主要参与蛋白质neddylation修饰及泛素化调控。具体文献建议通过PubMed或Google Scholar以关键词“DCUN1D4 recombinant protein”“neddylation”或“Cullin ligase”检索近年研究。
DCUN1D4 (Defective in Cullin Neddylation 1 Domain Containing 4) is a protein implicated in the regulation of cullin-RING ubiquitin ligases (CRLs), a critical family of E3 ubiquitin ligases involved in protein ubiquitination and degradation. It belongs to the DCUN1 protein family, characterized by a conserved DCUN1 domain that facilitates interactions with cullin scaffolds. DCUN1D4 specifically functions as a positive regulator of cullin neddylation, a post-translational modification essential for CRL complex activation. By promoting the transfer of NEDD8 (a ubiquitin-like protein) to cullins, DCUN1D4 enhances CRL-mediated substrate ubiquitination, thereby influencing diverse cellular processes such as cell cycle progression, DNA repair, and signal transduction.
Recombinant DCUN1D4 protein is engineered for in vitro studies to dissect its biochemical roles. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it retains functional domains necessary for binding cullins and modulating neddylation. Researchers utilize this purified protein to investigate its structural interactions, enzymatic kinetics, and regulatory mechanisms in CRL pathways. Mutagenesis studies on recombinant DCUN1D4 have identified residues critical for its activity, offering insights into how dysregulation of neddylation contributes to diseases like cancer, where CRL dysfunction is often observed.
Interest in DCUN1D4 also stems from its potential as a therapeutic target. Aberrant CRL activity is linked to tumorigenesis, and small molecules targeting neddylation pathways are under exploration. Recombinant DCUN1D4 enables high-throughput screening for inhibitors or stabilizers of its function. Additionally, its role in protein homeostasis and stress response pathways highlights broader implications in neurodegenerative and inflammatory diseases. Overall, DCUN1D4 recombinant protein serves as a vital tool for unraveling the complexities of ubiquitin-proteasome regulation and developing targeted therapies.
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