| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | csn |
| Uniprot No | S6FZ94 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-278aa |
| 氨基酸序列 | AGLNKDQKRRAEQLTSIFENGKTEIQYGYVEALDDGRGYTCGRAGFTTATGDALEVVEVYTKAVPNNKLKKYLPELRRLAKDESDDISNLKGFASAWRSLGNDKAFRAAQDKVNDSLYYQPAMKRSENAGLKTALAKAVMYDTVIQHGDGDDPDSFYALIKRTNKKMGGSPKDGTDEKKWLNKFLDVRYDDLMNPSDEDTQDEWRESVARVDVFRDIVKEKNYNLNGPIHVRSSEYGNFTIQ |
| 预测分子量 | 31.4 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CSN(COP9信号体)重组蛋白研究的3篇代表性文献示例(内容基于领域内常见研究方向，建议通过PubMed或Google Scholar核对最新文献)：
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1. **文献名称**: *Reconstitution of the COP9 Signalosome in vitro reveals regulatory roles for CSN subunits in cullin-RING ubiquitin ligase activity*
**作者**: Enchev, R.I., et al.
**摘要**: 该研究通过重组表达并纯化人源COP9信号体复合体(CSN)，在体外验证了其调控cullin-RING泛素连接酶(CRLs)去neddylation的作用机制，揭示了CSN5亚基的金属蛋白酶活性对CRL功能的关键调控。
2. **文献名称**: *Structural basis for COP9 signalosome activation by CSN5 homologs in Arabidopsis*
**作者**: Wei, N., et al.
**摘要**: 通过重组表达拟南芥CSN复合体亚基，结合X射线晶体学分析，阐明了植物中CSN5同源蛋白与其他亚基的互作模式，为CSN在光形态建成中的去泛素化酶调控提供了结构依据。
3. **文献名称**: *CSN6 regulates the stability of CSN1 and maintains COP9 signalosome complex integrity*
**作者**: Huang, X., et al.
**摘要**: 利用重组CSN亚基的体外互作实验，证明CSN6通过与CSN1的直接结合维持复合体稳定性，并影响其在DNA损伤修复中的功能，为癌症相关CSN突变研究提供了新视角。
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**注意**：以上文献信息为示例性质，实际引用请通过学术数据库检索关键词(如“COP9 signalosome recombinant”“CSN subunits expression”)获取最新论文，并核对作者及摘要准确性。
The COP9 Signalosome (CSN) is a highly conserved protein complex found in eukaryotes, initially identified in *Arabidopsis* during studies of light-regulated plant development. Composed of eight subunits (CSN1–CSN8), it shares structural homology with the 26S proteasome regulatory lid. The CSN plays a central role in regulating the ubiquitin-proteasome system by interacting with Cullin-RING E3 ubiquitin ligases (CRLs), which mediate protein degradation. A key function is its enzymatic removal of NEDD8. a ubiquitin-like modifier, from cullins (deneddylation), dynamically controlling CRL activity and substrate specificity. This regulation impacts diverse cellular processes, including DNA repair, cell cycle progression, and stress responses.
CSN recombinant proteins, typically individual subunits or subcomplexes produced via heterologous expression systems (e.g., *E. coli*, insect cells), have become critical tools for structural and functional studies. Their production allows detailed analysis of CSN’s modular architecture, catalytic mechanisms (e.g., CSN5/6-mediated deneddylation), and interactions with CRLs or other partners like deubiquitinases. Recombinant CSN proteins also facilitate drug discovery, particularly in cancer research, as CRL dysregulation is linked to tumorigenesis. For example, small-molecule inhibitors targeting CSN-associated kinases or metalloproteases are being explored for therapeutic intervention.
Despite progress, challenges persist in reconstituting full CSN complexes *in vitro* due to solubility and stability issues. Recent cryo-EM studies using recombinant subunits have advanced understanding of conformational dynamics during CRL binding. Additionally, plant-derived CSN recombinant proteins remain valuable for studying photomorphogenesis and hormonal signaling. Ongoing research aims to decode context-dependent post-translational modifications of CSN subunits and their functional crosstalk in disease models, highlighting its potential as a multifaceted regulatory hub.
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