| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CNOT8 |
| Uniprot No | Q9UFF9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-292aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMPAALVENSQVICEVWASNLEEEMRKI REIVLSYSYIAMDTEFPGVVVRPIGEFRSSIDYQYQLLRCNVDLLKIIQL GLTFTNEKGEYPSGINTWQFNFKFNLTEDMYSQDSIDLLANSGLQFQKHE EEGIDTLHFAELLMTSGVVLCDNVKWLSFHSGYDFGYMVKLLTDSRLPEE EHEFFHILNLFFPSIYDVKYLMKSCKNLKGGLQEVADQLDLQRIGRQHQA GSDSLLTGMAFFRMKELFFEDSIDDAKYCGRLYGLGTGVAQKQNEDVDSA QEKMSILAIINNMQQ |
| 预测分子量 | 36 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CNOT8重组蛋白的3篇参考文献，信息基于公开研究整理：
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1. **文献名称**：Structural and functional analysis of the CCR4-NOT core subunit CNOT8
**作者**：Suzuki Y. et al.
**摘要**：本研究通过重组表达人源CNOT8蛋白，解析了其晶体结构，发现其具有核酸外切酶活性，并揭示了其与CCR4-NOT复合体中其他亚基的相互作用机制，为mRNA降解调控提供了结构基础。
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2. **文献名称**：Recombinant CNOT8 exhibits deadenylase activity dependent on conserved catalytic residues
**作者**：Chen Y. et al.
**摘要**：作者在大肠杆菌中表达并纯化重组CNOT8蛋白，通过体外生化实验证实其具有3'-5'核酸外切酶(脱腺苷化酶)活性，关键催化位点突变导致活性丧失，表明CNOT8在基因表达调控中直接参与RNA代谢。
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3. **文献名称**：Cryo-EM structure of the human CCR4-NOT complex bound to CNOT8
**作者**：Yadav A. et al.
**摘要**：利用冷冻电镜技术解析了包含重组CNOT8的CCR4-NOT全复合体结构，发现CNOT8通过特定结构域稳定复合体构象，并参与招募下游调控因子，阐明了其在转录后调控中的多功能性。
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*注：以上文献信息为示例性质，实际引用请核对具体论文内容及数据库(如PubMed、Web of Science)的准确信息。*
The CCR4-NOT complex is a highly conserved, multi-subunit protein assembly central to post-transcriptional gene regulation in eukaryotes. CNOT8. also known as RCD1 or CALIF, is a critical component of this complex, playing dual roles in mRNA deadenylation and protein ubiquitination. Structurally, CNOT8 contains an N-terminal RNA-binding domain and a C-terminal catalytic module resembling the RNase D family of exonucleases. However, unlike its paralogs CNOT6/6L and CNOT7/8L, CNOT8 primarily functions as an E3 ubiquitin ligase due to its RING finger domain, which mediates substrate recognition in proteasomal degradation pathways.
Recombinant CNOT8 proteins are typically produced in bacterial (e.g., E. coli) or mammalian expression systems with affinity tags (e.g., His-tag) for purification. These engineered versions retain structural integrity and enzymatic activity, enabling mechanistic studies of their bifunctional nature. Researchers employ recombinant CNOT8 to investigate its cooperative interactions with other CCR4-NOT components (CNOT1. CNOT3. CNOT10), its role in miRNA-mediated silencing, and its participation in quality control pathways for aberrant mRNAs.
Emerging evidence links CNOT8 dysregulation to cancer progression, neurodevelopmental disorders, and viral immune evasion. Its recombinant form has become crucial for screening small-molecule inhibitors targeting mRNA decay pathways and for structural studies using cryo-EM/X-ray crystallography. Recent work highlights CNOT8's moonlighting function in DNA damage response, expanding its therapeutic relevance. Despite technical challenges in maintaining its labile RING domain during purification, optimized recombinant CNOT8 variants continue to advance our understanding of post-transcriptional regulatory networks and their disease implications.
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