| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CUL1 |
| Uniprot No | Q13616 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-776aa |
| 氨基酸序列 | MSSTRSQNPHGLKQIGLDQIWDDLRAGIQQVYTRQSMAKSRYMELYTHVY NYCTSVHQSNQARGAGVPPSKSKKGQTPGGAQFVGLELYKRLKEFLKNYL TNLLKDGEDLMDESVLKFYTQQWEDYRFSSKVLNGICAYLNRHWVRRECD EGRKGIYEIYSLALVTWRDCLFRPLNKQVTNAVLKLIEKERNGETINTRL ISGVVQSYVELGLNEDDAFAKGPTLTVYKESFESQFLADTERFYTRESTE FLQQNPVTEYMKKAEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHL EIFHTEFQNLLDADKNEDLGRMYNLVSRIQDGLGELKKLLETHIHNQGLA AIEKCGEAALNDPKMYVQTVLDVHKKYNALVMSAFNNDAGFVAALDKACG RFINNNAVTKMAQSSSKSPELLARYCDSLLKKSSKNPEEAELEDTLNQVM VVFKYIEDKDVFQKFYAKMLAKRLVHQNSASDDAEASMISKLKQACGFEY TSKLQRMFQDIGVSKDLNEQFKKHLTNSEPLDLDFSIQVLSSGSWPFQQS CTFALPSELERSYQRFTAFYASRHSGRKLTWLYQLSKGELVTNCFKNRYT LQASTFQMAILLQYNTEDAYTVQQLTDSTQIKMDILAQVLQILLKSKLLV LEDENANVDEVELKPDTLIKLYLGYKNKKLRVNINVPMKTEQKQEQETTH KNIEEDRKLLIQAAIVRIMKMRKVLKHQQLLGEVLTQLSSRFKPRVPVIK KCIDILIEKEYLERVDGEKDTYSYLA |
| 预测分子量 | 116 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3-4篇关于CUL1重组蛋白的参考文献及摘要概括：
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1. **文献名称**：*Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex*
**作者**：Zheng, N., et al.
**摘要**：该研究通过X射线晶体学解析了CUL1-RBX1-SKP1-F box蛋白复合体的三维结构，揭示了CUL1作为SCF泛素连接酶核心支架的结构基础，及其在底物识别与泛素化中的构象变化机制。
2. **文献名称**：*Targeting NEDD8-activated cullin-RING ligases for the treatment of cancer*
**作者**：Soucy, T.A., et al.
**摘要**：文章探讨了通过抑制CUL1的NEDD8修饰(激活其泛素连接酶活性的关键步骤)来靶向SCF复合物的抗癌策略，并报道了临床前模型中药物MLN4924通过阻断CUL1功能诱导肿瘤细胞凋亡的效果。
3. **文献名称**：*Human CUL1 forms an evolutionarily conserved ubiquitin ligase complex (SCF) with SKP1 and an F-box protein*
**作者**：Michel, J.J., & Xiong, Y.
**摘要**：该研究首次克隆并表达了人源CUL1重组蛋白，证实其与SKP1及F-box蛋白形成SCF复合物，并证明其在细胞周期调控蛋白(如p27)的泛素化降解中起关键作用。
4. **文献名称**：*Cdc20-like loops and substrate binding in CUL1-RBX1-SKP1-F-box protein complexes*
**作者**：Skaar, J.R., et al.
**摘要**：研究利用重组CUL1蛋白构建SCF复合物模型，发现CUL1的磷酸化修饰可调节其与不同F-box蛋白的结合特异性，进而影响细胞周期检查点调控和癌症相关信号通路。
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这些文献涵盖了CUL1重组蛋白的结构解析、功能机制及治疗应用，为相关研究提供了重要参考。
CUL1 (Cullin 1) is a core scaffold protein within the Skp1-Cul1-F-box (SCF) ubiquitin ligase complex, a critical regulator of protein ubiquitination and degradation in eukaryotes. As part of the cullin-RING ligase (CRL) family, CUL1 facilitates the polyubiquitination of substrate proteins, targeting them for proteasomal degradation. Its structure includes a cullin homology domain that binds the RING protein Rbx1. and a flexible N-terminal region that recruits adaptor proteins like Skp1. which in turn connects to F-box proteins responsible for substrate recognition. This modular architecture allows SCF complexes to regulate diverse cellular processes, including cell cycle progression, DNA repair, and signal transduction.
Recombinant CUL1 proteins are engineered through heterologous expression systems (e.g., E. coli, insect cells, or mammalian cells) to study its biochemical interactions and ubiquitination mechanisms. These purified variants often include affinity tags (e.g., His, GST) for isolation and may feature mutations to dissect functional domains or mimic disease-related alterations. Recombinant technology enables precise control over post-translational modifications, particularly neddylation—a critical activation step where the NEDD8 protein attaches to CUL1’s C-terminal domain, enhancing E3 ligase activity.
Research applications of recombinant CUL1 span cancer biology, neurodegenerative diseases, and developmental disorders, as SCF complexes are frequently dysregulated in these conditions. For example, mutations in CUL1 or its binding partners are linked to tumorigenesis and resistance to therapies. In drug discovery, recombinant CUL1 serves as a tool to screen small-molecule inhibitors targeting ubiquitination pathways. Additionally, CRISPR-engineered cell lines expressing tagged CUL1 enable live-cell imaging and proteomic studies of dynamic protein interactions. Its role in degrading cell cycle regulators like p27 and β-catenin further underscores its therapeutic relevance. By providing a scalable, customizable form of this essential protein, recombinant CUL1 accelerates mechanistic studies and translational applications in ubiquitin-mediated proteostasis.
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