| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SENP2 |
| Uniprot No | Q9HC62 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 360-589aa |
| 氨基酸序列 | RRTDDLLELTEDMEKEISNALGHGPQDEILSSAFKLRITRGDIQTLKNYH WLNDEVINFYMNLLVERNKKQGYPALHVFSTFFYPKLKSGGYQAVKRWTK GVNLFEQEIILVPIHRKVHWSLVVIDLRKKCLKYLDSMGQKGHRICEILL QYLQDESKTKRNSDLNLLEWTHHSMKPHEIPQQLNGSDCGMFTCKYADYI SRDKPITFTQHQMPLFRKKMVWEILHQQLL |
| 预测分子量 | 28 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SENP2重组蛋白的3篇示例参考文献(内容为模拟概括，建议通过学术数据库验证具体信息)：
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1. **文献名称**: *"SUMO-specific protease 2 is essential for modulating p53-Mdm2 in response to DNA damage"*
**作者**: Yeh, E. T. H., et al.
**摘要**: 本研究利用重组SENP2蛋白，揭示了其在DNA损伤应答中通过去SUMO化调控p53-Mdm2通路的关键作用。实验表明，重组SENP2能特异性切割SUMO修饰的Mdm2.从而稳定p53并促进细胞凋亡。
2. **文献名称**: *"Expression, purification, and enzymatic characterization of recombinant SENP2"*
**作者**: Mikolajczyk, J., et al.
**摘要**: 报道了SENP2重组蛋白在大肠杆菌中的高效表达及镍柱纯化方法，并通过体外酶活实验证明其特异性去SUMO化活性，为后续功能研究提供了可靠工具。
3. **文献名称**: *"Structural basis for SENP2 protease specificity towards SUMO isoforms"*
**作者**: Li, S. J., & Hochstrasser, M.
**摘要**: 通过晶体结构解析重组SENP2蛋白与SUMO1/SUMO2的复合物，阐明了其对不同SUPO亚型的选择性机制，为设计靶向SENP2的抑制剂提供了结构基础。
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**建议**：通过PubMed、Google Scholar或Web of Science搜索关键词“SENP2 recombinant protein”或“SENP2 expression”获取真实文献。
**Background of SENP2 Recombinant Protein**
Sentrin/SUMO-specific protease 2 (SENP2) is a member of the SENP (SUMO-specific protease) family, which plays a critical role in regulating post-translational modifications mediated by Small Ubiquitin-like Modifier (SUMO) proteins. SUMOylation, the covalent attachment of SUMO to target proteins, is a dynamic process involved in diverse cellular processes, including transcriptional regulation, nuclear transport, chromatin remodeling, and DNA repair. This modification is reversible, and SENP proteases are responsible for cleaving SUMO moieties from substrates or processing precursor SUMO proteins into their mature forms.
SENP2 localizes primarily to the nuclear envelope and nucleoplasm. Structurally, it contains a conserved C-terminal catalytic domain responsible for its protease activity and an N-terminal regulatory region that influences substrate specificity and subcellular localization. SENP2 exhibits dual functionality: it processes immature SUMO precursors (SUMO1. SUMO2/3) into their active forms by cleaving C-terminal tails and catalyzes deSUMOylation by removing SUMO from conjugated proteins.
Recombinant SENP2 protein is engineered for in vitro studies to investigate SUMO pathway dynamics. It is typically produced using expression systems like *E. coli* or mammalian cells, followed by purification via affinity chromatography. Researchers utilize SENP2 recombinant protein to dissect SUMO-mediated signaling pathways, study protein-protein interactions, or modulate SUMOylation in experimental models.
Dysregulation of SENP2 has been linked to diseases such as cancer, neurodegeneration, and cardiovascular disorders, highlighting its therapeutic potential. For instance, SENP2-mediated deSUMOylation of substrates like hypoxia-inducible factors (HIFs) or p53 influences tumor progression and stress responses. Its recombinant form thus serves as a vital tool for probing SUMO-related mechanisms and developing targeted therapies.
In summary, SENP2 recombinant protein is essential for understanding the SUMOylation-deSUMOylation equilibrium, offering insights into cellular homeostasis and disease pathogenesis.
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