| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CUL9 |
| Uniprot No | Q8IWT3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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CUL9重组蛋白的3篇示例参考文献(注：部分信息为示例性概括，建议通过学术数据库核实具体文献)：
1. **文献名称**: "CUL9 maintains genomic stability by regulating the ubiquitination and degradation of Aurora B"
**作者**: Zhao, J., et al.
**摘要**: 本研究利用重组CUL9蛋白进行体外泛素化实验，揭示了CUL9通过调控Aurora B激酶的泛素化降解，参与细胞有丝分裂的准确性维持，从而防止染色体不稳定性的发生。
2. **文献名称**: "Structural characterization of the CUL9-PPP1R12A complex by cryo-EM"
**作者**: Chen, X., et al.
**摘要**: 通过重组表达CUL9与其结合蛋白PPP1R12A，结合冷冻电镜技术解析了复合体三维结构，阐明了CUL9在调控磷酸酶活性中的构象变化机制。
3. **文献名称**: "CUL9 interacts with p53 to promote DNA damage-induced apoptosis"
**作者**: Wang, T., et al.
**摘要**: 利用重组CUL9蛋白进行互作实验，证实CUL9在DNA损伤条件下与p53直接结合，增强p53的转录活性，进而促进肿瘤细胞凋亡，为靶向治疗提供新思路。
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**备注**：以上文献信息为基于CUL9已知功能的模拟概括，实际文献需通过PubMed、Web of Science等平台检索关键词(如“CUL9 recombinant”“CUL9 ubiquitin”)获取。CUL9研究多集中于其E3泛素连接酶功能及在肿瘤、基因组稳定性中的作用。
CUL9 (Cullin 9), also known as PARC or p53-associated Parkin-like cytoplasmic protein, is a member of the cullin family of scaffold proteins that play critical roles in ubiquitin-mediated protein degradation. Unlike other cullins, CUL9 lacks a canonical cullin homology domain but contains an APC2/β domain and a Parkin-like ubiquitin ligase region, enabling its involvement in unique protein ubiquitination pathways. It was initially identified as a cytoplasmic binding partner of the tumor suppressor p53. where it sequesters p53 in the cytoplasm under non-stress conditions, modulating its nuclear functions in apoptosis and cell cycle regulation. CUL9 also interacts with the retinoblastoma protein (pRb) and other regulators of genomic stability, suggesting roles in tumor suppression and DNA damage response.
Recombinant CUL9 protein is engineered for in vitro studies to elucidate its structural and functional properties. Produced via heterologous expression systems (e.g., E. coli, mammalian cells), it retains key domains for protein-protein interactions and ubiquitin ligase activity. Researchers utilize recombinant CUL9 to investigate its E3 ligase mechanisms, substrate specificity, and regulatory roles in cellular processes like autophagy, apoptosis, and oncogenesis. Its ability to form dynamic complexes with p53. pRb, and ubiquitin enzymes makes it a focal point in cancer biology, particularly in understanding how dysregulation of ubiquitination contributes to tumor progression. Challenges in studying CUL9 include its large size (~250 kDa), post-translational modifications, and context-dependent interactions. Current efforts aim to map its interactome, characterize its ligase activity, and explore therapeutic targeting of CUL9-associated pathways in diseases linked to protein homeostasis defects.
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