| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRMT1 |
| Uniprot No | Q99873-3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-343aa |
| 氨基酸序列 | MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK DEVRTLTYRN SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE CSSISDYAVK IVKANKLDHV VTIIKGKVEE VELPVEKVDI IISEWMGYCL FYESMLNTVL YARDKWLAPD GLIFPDRATL YVTAIEDRQY KDYKIHWWEN VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY TVKVEDLTFT SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY RMR |
| 预测分子量 | 68 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PRMT1重组蛋白的3篇参考文献，包含文献名称、作者及摘要内容概括：
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1. **文献名称**：*Protein arginine methyltransferases and cancer*
**作者**：Mark T. Bedford, Steven G. Clarke
**摘要**：该综述系统总结了PRMT家族(包括PRMT1)的功能及其在癌症中的作用，强调了重组PRMT1蛋白在体外研究中的应用，如底物甲基化机制和酶动力学分析，为靶向治疗提供了理论基础。
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2. **文献名称**：*Structure and function of protein arginine methyltransferase PRMT1*
**作者**：Jian Tang, Andrew P. Waters, Gary D. Glick
**摘要**：本研究利用重组人源PRMT1蛋白解析其晶体结构，揭示了催化核心区域的关键氨基酸残基及其底物结合模式，阐明了精氨酸甲基化反应的分子机制。
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3. **文献名称**：*PRMT1 regulates tumor cell plasticity and stemness via histone H4 arginine methylation*
**作者**：Hua Wei, Kuangyu Yen, Yue Chen
**摘要**：通过重组PRMT1蛋白进行体外甲基化实验，证明其通过组蛋白H4的R3位点甲基化调控肿瘤干细胞的可塑性，并验证了其在乳腺癌细胞中的促癌功能。
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4. **文献名称**：*Substrate specificity of PRMT1: Role of dimerization and co-activator binding*
**作者**：Yanzhong Yang, Mark T. Bedford
**摘要**：研究利用重组PRMT1蛋白结合质谱技术，鉴定了其特异性底物结合域，并发现二聚化对酶活性的调控作用，揭示了PRMT1在信号转导中的选择性机制。
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这些文献覆盖了PRMT1重组蛋白的结构、功能、机制及疾病关联研究，可作为相关研究的参考基础。
PRMT1 (Protein Arginine Methyltransferase 1) is a pivotal enzyme in eukaryotic cells responsible for catalyzing the post-translational methylation of arginine residues on histones and non-histone proteins. As the predominant type I arginine methyltransferase, it transfers methyl groups from S-adenosylmethionine (SAM) to specific arginine residues, generating monomethylarginine (MMA) and asymmetric dimethylarginine (aDMA). This modification regulates diverse cellular processes including transcriptional regulation, DNA repair, RNA processing, and signal transduction. PRMT1 is particularly notable for its role in epigenetics through methylation of histone H4 at arginine 3 (H4R3me2a), a modification linked to chromatin remodeling and gene activation.
Structurally, PRMT1 contains a conserved catalytic core with a SAM-binding domain and substrate recognition motifs. Its activity depends on dimerization and interactions with regulatory partners. Recombinant PRMT1 proteins, typically produced in E. coli or mammalian expression systems, retain enzymatic activity and are essential tools for studying methylation mechanisms. Purification methods often involve affinity tags (e.g., GST or His-tag) followed by size-exclusion chromatography to ensure homogeneity.
Research has implicated PRMT1 in various diseases, particularly cancer. It promotes oncogenesis by methylating substrates like RUNX1. EGFR, and FOXO1. influencing cell proliferation and apoptosis. Aberrant PRMT1 expression correlates with leukemia, breast cancer, and lung cancer progression. In neurodegenerative disorders, PRMT1-mediated methylation modulates TDP-43 aggregation and stress granule dynamics. Additionally, its role in metabolic diseases involves lipid metabolism regulation through PPARγ methylation.
The development of PRMT1-specific inhibitors (e.g., MS023. GSK3368715) highlights its therapeutic potential. Recombinant PRMT1 enables high-throughput drug screening and mechanistic studies, providing insights into substrate specificity and methylation crosstalk with other post-translational modifications. Its conserved function across species and versatile applications in biochemistry make it a critical target for both basic research and pharmaceutical development.
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