| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SUMO2 |
| Uniprot No | P61956 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-93aa |
| 氨基酸序列 | MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCER QGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGG |
| 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. |
1. **"SUMO modification of the ubiquitin-conjugating enzyme E2-25K"**
- *作者：Matic I, et al.*
- 摘要：研究利用重组SUMO2蛋白验证其在体外泛素化反应中的调控作用，揭示了SUMO2修饰对E2-25K酶活性的影响及可能的交叉调控机制。
2. **"In vitro SUMO-2 conjugation using recombinant enzymes"**
- *作者：Knipscheer P, et al.*
- 摘要：开发了一种基于重组SUMO2蛋白的体外偶联系统，阐明了SUMO2结合酶(E1/E2/E3)的催化机制及其底物特异性，为研究SUMOylation通路提供工具。
3. **"Crystal structure of the SUMO2 protein from human"**
- *作者：Baba D, et al.*
- 摘要：通过重组表达纯化人源SUMO2蛋白，解析其高分辨率晶体结构，揭示了SUMO2与其他SUMO亚型(如SUMO1)的结构差异及功能关联。
4. **"SUMO2 modification of tau protein in neurodegenerative diseases"**
- *作者：Yun SM, et al.*
- 摘要：利用重组SUMO2蛋白在细胞模型中研究Tau蛋白的SUMO化修饰，发现其通过调控Tau聚集影响阿尔茨海默病的病理进程。
(注：上述文献信息为示例性内容，实际引用需核对具体论文细节。)
SUMO2 (Small Ubiquitin-like Modifier 2) is a member of the SUMO protein family, which plays a critical role in post-translational modification processes. Similar to ubiquitin, SUMO proteins conjugate to target proteins through a cascade of enzymatic reactions (E1 activating, E2 conjugating, and E3 ligating enzymes), a process termed SUMOylation. This modification regulates diverse cellular functions, including protein localization, stability, transcriptional regulation, DNA repair, and stress responses. Among SUMO paralogs (SUMO1-4), SUMO2 shares ~50% sequence identity with SUMO1 but exhibits unique dynamics, such as forming poly-SMO chains under stress conditions.
Recombinant SUMO2 protein is engineered for research and therapeutic applications. It is typically produced in bacterial systems (e.g., E. coli) or eukaryotic expression systems to ensure proper folding and post-translational modifications. The recombinant form retains the conserved structural features of native SUMO2. including the diglycine motif required for conjugation and a C-terminal tail processed by SUMO-specific proteases. Its small size (~11 kDa) and solubility make it ideal for in vitro studies, such as investigating SUMOylation mechanisms, enzyme kinetics, or protein-protein interactions.
SUMO2 recombinant protein is widely used to enhance the solubility and stability of fusion partners during recombinant protein expression. Additionally, it serves as a substrate for developing SUMOylation assays or inhibitors. In drug discovery, SUMO2 fusion tags are leveraged to improve the yield of difficult-to-express proteins. The reversible nature of SUMOylation, mediated by SENP proteases, allows precise control in experimental workflows. Its role in neurodegenerative diseases, cancer, and immune regulation further drives its utility in biomedical research.
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