| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRMT3 |
| Uniprot No | Q8WUV3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-531aa |
| 氨基酸序列 | MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPC LFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKN PTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPN GLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVR TCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQN PHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLN KLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAK NKYLAKGGSVYPDICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAV IPEAVVEVLDPKTLISEPCGIKHIDCHTTSISDLEFSSDFTLKITRTSMC TAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTVFLLEKPFSVKAGEA LKGKVTVHKSKKDPRSLTVTLTLNNSTQTYGLQ |
| 预测分子量 | 97 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3-4条关于PRMT3重组蛋白的参考文献及简要摘要：
1. **"Crystal Structure of the C-terminal Domain of Human Protein Arginine Methyltransferase 3"**
*作者：Tanner, K.G. et al. (2000)*
摘要：报道了人源PRMT3 C端结构域的晶体结构，阐明了其锌离子结合位点的结构特征，并揭示了该结构域对酶活性的调控作用。
2. **"Structural Basis for Substrate Recognition by Protein Arginine Methyltransferase 3"**
*作者：Frankel, A. et al. (2005)*
摘要：通过重组PRMT3蛋白的生化分析及底物结合实验，揭示了PRMT3对核糖体蛋白S2(RPS2)的选择性甲基化机制及其底物结合口袋的结构特征。
3. **"PRMT3 Regulates Ribosomal RNA Biogenesis through Methylation of Histone H4"**
*作者：Singh, S. et al. (2019)*
摘要：利用重组PRMT3蛋白进行体外甲基化实验，发现其通过催化组蛋白H4的特定精氨酸甲基化，调控核糖体RNA合成及细胞增殖功能。
4. **"PRMT3-Mediated Arginine Methylation in Cancer Progression"**
*作者：Deng, X. et al. (2021)*
摘要：通过重组PRMT3蛋白的功能研究，揭示了其在肺癌中通过甲基化修饰转录因子STAT3.促进肿瘤细胞迁移和侵袭的分子机制。
注：以上文献标题和作者为简化示例，实际引用需核对具体论文信息。
**Background of PRMT3 Recombinant Protein**
Protein arginine methyltransferase 3 (PRMT3) is a member of the PRMT family, which catalyzes the post-translational methylation of arginine residues in proteins, playing critical roles in epigenetic regulation, signal transduction, and cellular homeostasis. PRMT3 specifically mediates asymmetric dimethylation of arginine (ADMA), a modification that influences protein-protein interactions, subcellular localization, and functional activity of target substrates. Structurally, PRMT3 contains a catalytic core domain conserved across PRMTs and a unique N-terminal zinc-finger domain implicated in substrate recognition and binding.
Recombinant PRMT3 is generated through heterologous expression systems (e.g., *E. coli* or mammalian cells) followed by purification to homogeneity. This engineered protein retains enzymatic activity and is widely used to study methylation mechanisms, substrate specificity, and regulatory roles in biological processes. A well-characterized substrate of PRMT3 is the ribosomal protein S2 (RPS2), where methylation modulates ribosome biogenesis and translation efficiency. PRMT3 also interacts with other targets, including histones and non-histone proteins, linking it to transcriptional regulation, RNA processing, and stress responses.
Dysregulation of PRMT3 is associated with diseases such as cancer, neurodevelopmental disorders, and metabolic syndromes. For instance, PRMT3 overexpression has been observed in hepatocellular carcinoma, while its deficiency impacts neural development in models of intellectual disability. Recombinant PRMT3 serves as a vital tool for drug discovery, enabling high-throughput screening of inhibitors targeting PRMT3-driven pathologies. Additionally, structural studies using recombinant PRMT3 have provided insights into its mechanism, aiding the design of selective therapeutics. Overall, PRMT3 recombinant protein bridges molecular research and translational applications, advancing our understanding of arginine methylation in health and disease.
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