| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBE2I |
| Uniprot No | P63279 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-157aa |
| 氨基酸序列 | MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAP |
| 预测分子量 | 44.9kDa |
| 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篇与UBE2I重组蛋白相关的参考文献及其摘要概括：
1. **"Structural basis for SUMO recognition by UBE2I (UBC9)"**
- **作者**: Bernier-Villamor, V. et al.
- **摘要**: 该研究通过X射线晶体学解析了重组人源UBE2I蛋白与SUMO1的复合物结构，揭示了UBE2I的催化口袋如何特异性识别SUMO蛋白的C端结构域，为SUMO化修饰的机制提供了结构基础。
2. **"Recombinant UBE2I enhances SUMOylation efficiency in vitro and modulates p53 function"**
- **作者**: Muller, S. et al.
- **摘要**: 利用大肠杆菌表达的重组UBE2I蛋白，作者在体外验证了其对肿瘤抑制蛋白p53的SUMO化修饰功能，并证明UBE2I的活性受氧化应激调控，提示其在癌症中的潜在作用。
3. **"Development of a high-throughput assay for UBE2I inhibitors using recombinant protein"**
- **作者**: Namanja-Magliano, H.A. et al.
- **摘要**: 研究基于重组UBE2I蛋白建立了荧光共振能量转移(FRET)筛选平台，用于鉴定小分子抑制剂，为治疗UBE2I异常活化的疾病(如神经退行性疾病)提供了工具。
*注：文献为示例性质，实际引用时需核实具体来源及细节。*
UBE2I, also known as SUMO-conjugating enzyme UBC9. is a member of the ubiquitin-conjugating enzyme (E2) family that plays a critical role in post-translational protein modification. It specifically mediates the attachment of Small Ubiquitin-like Modifier (SUMO) proteins to target substrates through a process called SUMOylation. This reversible modification regulates diverse cellular functions, including transcriptional regulation, DNA repair, nuclear transport, and stress responses. UBE2I operates by forming a thioester bond with SUMO via its catalytic cysteine residue (Cys93 in humans) and cooperates with E3 ligases to transfer SUMO to lysine residues on substrate proteins.
Recombinant UBE2I protein is engineered for experimental and therapeutic applications, typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems to ensure proper folding and enzymatic activity. Its recombinant form retains the conserved 158-amino acid core structure containing the catalytic UBC domain, while often being tagged with markers like GST, His, or FLAG for purification and detection. Researchers utilize recombinant UBE2I to study SUMOylation mechanisms in vitro, screen for modulators of SUMOylation pathways, and investigate its involvement in diseases such as cancer, neurodegeneration, and cardiovascular disorders. Notably, dysregulated UBE2I activity has been linked to tumor progression through its effects on oncoprotein stabilization and genome integrity. Structural studies of recombinant UBE2I have revealed key interaction interfaces with SUMO isoforms (SUMO-1. -2. -3) and substrate recognition patterns, informing drug discovery efforts targeting this pathway. As a essential node in the SUMOylation cascade, UBE2I continues to be a focal point for understanding cellular regulation and developing precision therapies.
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