Recombinant Human SUMO1 protein

中文名： 间隙修饰蛋白1(SUMO1)重组蛋白
别名： SUMO1；SMT3C；Small ubiquitin-related modifier 1

货号: PA1000-3082

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	SUMO1
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.

参考文献

以下是关于SUMO1重组蛋白的3篇参考文献示例(内容基于领域知识合理构建，具体文献需通过数据库验证)：

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1. **文献名称**：*"High-Yield Expression and Purification of Recombinant Human SUMO1 for Functional Studies"*

**作者**：Lee, S.J. et al.

**摘要**：该研究报道了一种在大肠杆菌中高效表达和纯化重组人SUMO1蛋白的优化方法，通过亲和层析和尺寸排阻色谱获得高纯度蛋白，并验证其在体外SUMOylation反应中的功能活性。

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2. **文献名称**：*"Structural Basis for SUMO1 Recognition by SENP1 Protease"*

**作者**：Li, H. & Chen, Y.

**摘要**：通过X射线晶体学解析了重组SUMO1蛋白与去SUMO化酶SENP1的复合物结构，揭示了SUMO1特异性识别的分子机制，为设计靶向SUMO通路的抑制剂提供了结构基础。

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3. **文献名称**：*"SUMO Fusion System Enhances Solubility and Stability of Heterologous Proteins in Mammalian Cells"*

**作者**：Malakhov, M.P. et al.

**摘要**：开发了一种基于SUMO1的融合蛋白表达系统，证明SUMO1标签能显著提高难溶性真核蛋白在哺乳动物细胞中的表达量和稳定性，简化了后续纯化流程。

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4. **文献名称**：*"A FRET-Based Screening Platform for Modulators of SUMO1 Conjugation"*

**作者**：Wang, Q. et al.

**摘要**：利用重组SUMO1和荧光共振能量转移(FRET)技术，构建了高通量筛选平台，成功鉴定出多个调控SUMO1与靶蛋白结合的化合物，为疾病治疗提供潜在工具。

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如需具体文献，建议通过PubMed或Google Scholar搜索关键词“SUMO1 recombinant protein expression”、“SUMO1 structural analysis”等获取最新研究。

背景信息

SUMO1 (Small Ubiquitin-like Modifier 1) is a member of the SUMO protein family, which plays a critical role in post-translational modification (PTM) processes. These modifications regulate diverse cellular functions, including protein localization, stability, activity, and interactions. SUMO proteins are structurally similar to ubiquitin but function independently, primarily through covalent conjugation to target proteins (SUMOylation) via a cascade of enzymatic steps involving E1 (activating), E2 (conjugating), and E3 (ligating) enzymes.

Recombinant SUMO1 protein is engineered through genetic expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to produce high-purity, functional SUMO1 for research and therapeutic applications. Its recombinant form retains the ability to participate in SUMOylation machinery, making it invaluable for *in vitro* studies of protein modification mechanisms, enzyme kinetics, and substrate identification. Researchers use it to investigate SUMO1’s role in cellular pathways such as DNA repair, transcriptional regulation, stress responses, and nuclear-cytoplasmic transport.

Structurally, recombinant SUMO1 typically includes affinity tags (e.g., His-tag, GST) for simplified purification and detection. It is often expressed in its mature form (cleaved from precursor proteins) or as fusion partners to enhance solubility of target proteins. Dysregulation of SUMO1 has been linked to neurodegenerative diseases, cancer, and viral infections, driving demand for recombinant tools in drug discovery and molecular diagnostics.

Additionally, SUMO1 recombinant proteins are used to develop SUMO-specific proteases (SENPs) and inhibitors, aiding mechanistic studies and therapeutic targeting. Their standardized production ensures reproducibility in experiments, addressing challenges associated with endogenous SUMO1’s low abundance and rapid turnover in cells. Overall, recombinant SUMO1 serves as a cornerstone for unraveling SUMOylation’s complexity and its implications in health and disease.