| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RG9MTD1 |
| Uniprot No | Q7L0Y3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-252 aa |
| 活性数据 | MKAAAREEAKNIKLLETTEEDKQKNFLFLRLWDRNMDIAMGWKGAQAMQFGQPLVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVKRYQEKWDKLLLTSTEKSHVDLFPKDSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGTSLAKAKRLNLATECLPLDKYLQWEIGNKNLTLDQMIRILLCLKNNGNWQEALQFVPKRKHTGFLEISQHSQEFINRLKKAKT |
| 分子量 | 56 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下为与重组人RG9MTD1(假设为tRNA/rRNA甲基转移酶相关)蛋白相关的虚构参考文献示例，供参考(实际文献需通过专业数据库查询)：
1. **文献名称**：*Structural insights into human RG9MTD1 methyltransferase in tRNA modification*
**作者**：Chen L, et al.
**摘要**：本研究解析了RG9MTD1蛋白的晶体结构，揭示了其催化域对tRNA特定核苷酸的甲基化机制，并发现其突变可能影响RNA稳定性及翻译效率。
2. **文献名称**：*RG9MTD1 regulates ribosome biogenesis through 18S rRNA methylation*
**作者**：Wang Y, et al.
**摘要**：通过基因敲除实验，证明RG9MTD1通过催化18S rRNA甲基化调控核糖体生成，其功能缺失导致细胞增殖受损及蛋白质合成障碍。
3. **文献名称**：*High-yield expression and purification of recombinant human RG9MTD1 in E. coli*
**作者**：Zhang R, et al.
**摘要**：开发了一种高效重组RG9MTD1蛋白的大肠杆菌表达系统，优化纯化步骤后获得高活性蛋白，为后续酶学研究和抑制剂筛选奠定基础。
4. **文献名称**：*Dysregulation of RG9MTD1 in cancer: Implications for epigenetic therapy*
**作者**：Kim H, et al.
**摘要**：发现RG9MTD1在多种肿瘤中异常高表达，其过表达促进癌细胞侵袭，提示其作为表观遗传治疗靶点的潜力。
**注意**：以上内容属模拟文献，实际研究需通过PubMed、Google Scholar等平台以准确关键词(如“RG9MTD1”、“RNA methyltransferase”、“重组表达”)检索。若蛋白名称有误，建议核实基因官方符号(如确认是否为DIMT1/TRMT10C等类似甲基转移酶)。
Recombinant human RG9MTD1 protein is a genetically engineered protein of interest in RNA biology and post-transcriptional regulation. Its name likely derives from conserved structural motifs, such as an RG-rich (arginine-glycine) domain and a methyltransferase domain (MTD), though its exact nomenclature context remains unclear. RG9MTD1 is hypothesized to function as an RNA methyltransferase, potentially involved in modifying RNA molecules (e.g., m6A or other modifications) to regulate mRNA stability, splicing, or translation—key mechanisms in cellular processes like gene expression and stress responses.
Structurally, recombinant RG9MTD1 is typically produced using bacterial (e.g., *E. coli*) or eukaryotic expression systems, often fused with tags like His-tag for purification. Studies suggest its association with RNA-binding proteins and involvement in ribonucleoprotein complexes. While its precise biological roles are under investigation, emerging evidence links RNA methyltransferases to diseases such as cancer, neurodegenerative disorders, and viral infections, making RG9MTD1 a potential therapeutic target. Current research focuses on elucidating its substrate specificity, catalytic mechanisms, and interaction networks using techniques like crystallography and CRISPR-based functional assays. Further characterization may advance understanding of epitranscriptomics and RNA-centric disease pathways.
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