| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBE2F |
| Uniprot No | Q969M7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-185aa |
| 氨基酸序列 | MLTLASKLKRDDGLKGSRTAATASDSTRRVSVRDKLLVKEVAELEANLPC TCKVHFPDPNKLHCFQLTVTPDEGYYQGGKFQFETEVPDAYNMVPPKVKC LTKIWHPNITETGEICLSLLREHSIDGTGWAPTRTLKDVVWGLNSLFTDL LNFDDPLNIEAAEHHLRDKEDFRNKVDDYIKRYAR |
| 预测分子量 | 24 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UBE2F重组蛋白的模拟参考文献示例(注：以下内容为假设性示例，实际文献需通过学术数据库检索)：
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1. **文献名称**: *UBE2F-CRL5 Complex Mediates Neddylation-Dependent Protein Ubiquitination*
**作者**: Huang, D.T., Schulman, B.A.
**摘要**: 本研究解析了UBE2F重组蛋白与CRL5(Cullin-RING ligase 5)复合体的相互作用机制，证明UBE2F通过转移NEDD8修饰激活CRL5的泛素连接酶活性，进而促进底物蛋白的泛素化降解。实验利用重组UBE2F蛋白验证了其在体外泛素化级联反应中的关键作用。
2. **文献名称**: *Structural Insights into UBE2F-Specific Recognition by CRL5 Substrates*
**作者**: Zhao, Q., et al.
**摘要**: 通过X射线晶体学技术，该研究揭示了重组UBE2F蛋白与病毒蛋白HBx的结合界面结构，阐明了UBE2F在乙型肝炎病毒介导的宿主泛素化调控中的独特功能，为靶向UBE2F的抗病毒策略提供了结构基础。
3. **文献名称**: *UBE2F Recombinant Protein Enhances In Vitro Ubiquitination Assays for Drug Screening*
**作者**: Smith, J., et al.
**摘要**: 研究开发了一种基于重组UBE2F蛋白的高通量泛素化检测体系，用于筛选调控CRL5通路的小分子抑制剂。实验表明，UBE2F的活性对肿瘤细胞中特定癌蛋白的稳定性具有显著影响，为癌症治疗提供了潜在靶点。
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**提示**：以上文献为示例性质，实际研究中请通过**PubMed**、**Google Scholar**或**Web of Science**等平台，以关键词“UBE2F recombinant”“UBE2F ubiquitination”检索最新文献。若需具体论文协助，请提供更多研究背景信息。
UBE2F, a member of the ubiquitin-conjugating enzyme (UBC) family, plays a critical role in the ubiquitin-proteasome system (UPS), which regulates protein degradation and cellular homeostasis. This enzyme catalyzes the transfer of ubiquitin to substrate proteins, marking them for proteasomal degradation or functional modulation. UBE2F specifically interacts with cullin-RING ligases (CRLs), particularly Cullin-5 (CUL5), to mediate neddylation—a post-translational modification essential for CRL complex activation. Structurally, UBE2F contains a conserved catalytic core domain responsible for ubiquitin binding and a unique N-terminal extension that facilitates protein-protein interactions.
Recombinant UBE2F protein is engineered through heterologous expression systems (e.g., E. coli or mammalian cells) to enable functional and structural studies. Its production typically involves cloning the UBE2F gene into expression vectors, followed by purification via affinity chromatography. Recombinant versions retain enzymatic activity while offering advantages like high purity, solubility, and tagged variants for experimental tracking.
Research on recombinant UBE2F has shed light on its role in viral pathogenesis (e.g., HIV-1 restriction by modulating CUL5 complexes), cancer progression (via substrate-specific degradation pathways), and neurodegenerative diseases. Inhibitors targeting UBE2F-mediated neddylation are being explored as potential therapies. Additionally, structural studies using recombinant protein have revealed binding interfaces with E3 ligases and regulatory proteins, providing insights for drug design. As a tool molecule, it is widely used in in vitro ubiquitination assays and CRL activity reconstitution experiments.
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