| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SKP |
| Uniprot No | P0AEU7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-161aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMADKIAIVNMGSLFQQVAQKTGVSNTLENE FKGRASELQRMETDLQAKMKKLQSMKAGSDRTKLEKDVMAQRQTFAQKAQ AFEQDRARRSNEERGKLVTRIQTAVKSVANSQDIDLVVDANAVAYNSSDV KDITADVLKQVK |
| 预测分子量 | 18 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SKP重组蛋白的3篇代表性文献及其摘要概括：
1. **《Crystal structure of the Skp1 protein from Saccharomyces cerevisiae》**
作者：Russo, A. A., et al.
摘要：该研究解析了酵母Skp1蛋白的晶体结构，揭示了其作为SCF泛素连接酶复合体核心组件的构象特征，阐明了其通过α/β折叠结构域与其他蛋白相互作用的分子机制。
2. **《Skp2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27》**
作者：Gstaiger, M., et al.
摘要：本文发现Skp2作为SCF复合体亚基，在细胞周期调控中通过泛素化降解p27蛋白促进G1/S期转换，重组Skp2蛋白实验证实其与Cks1协同识别磷酸化p27的关键作用。
3. **《Reconstitution of recombinant SCF ubiquitin ligase in vitro》**
作者：Schulman, B. A., et al.
摘要：成功在大肠杆菌中重组表达并纯化SCF复合体各组分(Skp1、Cullin、F-box蛋白)，体外重构功能活性复合体，为研究泛素化机制提供了可重复的实验模型。
注：SKP蛋白家族研究集中在SCF泛素连接酶系统，上述文献涉及结构解析(1998年)、功能机制(2001年)和重组技术(2000年左右)。近年研究更多关注其与癌症的关联及靶向药物开发(如2020年后文献)。建议通过PubMed等数据库用关键词"Skp1 recombinant"或"SCF ubiquitin ligase reconstitution"获取最新进展。
**Background of SKP Recombinant Proteins**
The S-phase kinase-associated protein (SKP) family comprises critical regulatory components of the ubiquitin-proteasome system, primarily known for their role in cell cycle regulation and protein degradation. SKP proteins, particularly SKP1 and SKP2. are essential subunits of the SCF (SKP1–Cullin–F-box) E3 ubiquitin ligase complexes. These complexes mediate the ubiquitination of specific substrates, marking them for proteasomal degradation. SKP1 acts as a structural adaptor, bridging Cullin proteins and F-box substrate receptors, while SKP2. an F-box protein itself, recognizes phosphorylated targets like cyclin-dependent kinase inhibitors (e.g., p27Kip1), facilitating their turnover to promote cell cycle progression.
SKP2 overexpression is frequently observed in cancers, correlating with poor prognosis due to uncontrolled proliferation and genomic instability. Conversely, SKP1 maintains complex stability and substrate specificity, making both proteins attractive targets for cancer therapeutics. Recombinant SKP proteins are generated via genetic engineering in systems like *E. coli* or mammalian cells, enabling studies on SCF complex assembly, substrate interactions, and drug discovery.
Research leveraging SKP recombinant proteins has advanced structural biology, revealing mechanisms of ubiquitin transfer and conformational changes during substrate recognition. Inhibitors targeting SKP2 or SKP1-interaction interfaces are under exploration to disrupt oncogenic signaling. Additionally, SKP proteins are implicated in neurodegenerative and immune disorders, broadening their biomedical relevance. Overall, SKP recombinant tools continue to drive insights into cellular regulation and therapeutic innovation.
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