纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PCI |
Uniprot No | P05154 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-406aa |
氨基酸序列 | MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP |
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PCI重组蛋白的3篇参考文献,供参考:
1. **"Structural organization of the 19S proteasome lid: insights from MS of intact complexes"**
- **作者**: Groll, M. et al.
- **摘要**: 研究通过质谱和结构分析揭示了19S蛋白酶体调控颗粒中PCI结构域蛋白(如Rpn5、Rpn6等)的组装模式,阐明了其在底物识别和去泛素化中的作用。
2. **"The COP9 signalosome: a multifunctional regulator of PCI protein complexes"**
- **作者**: Wei, N. & Deng, X.W.
- **摘要**: 综述了COP9信号体(含PCI结构域)与蛋白酶体、eIF3等复合物的相互作用,重点讨论其在信号转导和蛋白质降解中的调控机制。
3. **"Crystal structure of the eIF3k-eIF3l subcomplex reveals a conserved PCI-core dimer in eukaryotic translation initiation"**
- **作者**: Sun, C. et al.
- **摘要**: 通过晶体学解析了真核翻译起始因子eIF3中PCI结构域亚基k/l的异源二聚体结构,揭示了其在复合物支架功能中的进化保守性。
4. **"Reconstitution and structural analysis of recombinant PCI complexes using cryo-EM"**
- **作者**: Sharon, M. et al.
- **摘要**: 利用冷冻电镜技术重构了重组PCI蛋白复合物(如PAN3/CCR4-NOT)的三维结构,揭示了其介导RNA代谢和转录调控的分子机制。
如需具体文献链接或更早/更新的研究,可进一步补充说明。
**Background of PCI Recombinant Proteins**
PCI recombinant proteins are engineered versions of proteins containing the PCI domain (Proteasome, COP9 signalosome, eIF3), a conserved structural motif critical for mediating protein-protein interactions in multisubunit complexes. The PCI domain, typically ~200 amino acids long, is found in subunits of three major eukaryotic complexes: the 26S proteasome, the COP9 signalosome (CSN), and the eukaryotic translation initiation factor 3 (eIF3). These complexes play pivotal roles in protein degradation, cellular signaling, and translation regulation, respectively.
The **proteasome** is a protease complex responsible for degrading ubiquitinated proteins, essential for maintaining protein homeostasis. The **COP9 signalosome** regulates ubiquitin ligases and is involved in light-mediated plant development and cell cycle control. **eIF3** facilitates ribosome recruitment during translation initiation. PCI-containing subunits within these complexes often serve as scaffolds, stabilizing interactions between regulatory and catalytic components.
Recombinant PCI proteins are generated via heterologous __expression (e.g., in *E. coli* or mammalian cells) to study their structural and functional roles. These proteins enable researchers to dissect molecular mechanisms, such as how PCI domains coordinate complex assembly or recruit substrates. For example, studies using recombinant CSN subunits have clarified their role in deneddylation, while proteasome PCI proteins have provided insights into substrate recognition.
PCI recombinant proteins also have therapeutic implications. Dysregulation of PCI-containing complexes is linked to cancers, neurodegenerative diseases, and immune disorders. Engineered PCI proteins aid in drug screening, structural analysis (e.g., crystallography, cryo-EM), and developing targeted therapies. Their modular nature and conserved interaction interfaces make them valuable tools for both basic research and biomedical applications.
In summary, PCI recombinant proteins are vital for understanding cellular regulation and developing interventions for diseases tied to proteostasis, signaling, or translation defects.
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