| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNMT |
| Uniprot No | O43148 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-476aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMANSAKAEEYEKMSLEQAKASVNSETESSF NINENTTASGTGLSEKTSVCRQVDIARKRKEFEDDLVKESSSCGKDTPSK KRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTGDGTQNKRKIA LEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMK SVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIAD VSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDI CSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEA SETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNE MAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEPYPANESSKLV SEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ |
| 预测分子量 | 57 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RNMT重组蛋白的3篇示例参考文献(注：以下文献信息为示例性概括，实际引用需核实准确性)：
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1. **文献名称**: "Structural basis of RNA cap modification by the RNMT enzyme complex"
**作者**: Taylor, N.M. et al.
**摘要**: 解析了重组人源RNMT与底物复合物的晶体结构，揭示了其催化mRNA 5'端加帽的分子机制及与激活子RAM的相互作用位点。
2. **文献名称**: "Recombinant RNMT demonstrates substrate specificity in mRNA cap methylation"
**作者**: Arecero-Curiel, R. et al.
**摘要**: 利用重组RNMT蛋白进行体外酶活实验，证明其对RNA链长度及5'端结构的依赖性，并发现其甲基化活性受翻译起始因子调控。
3. **文献名称**: "Targeting RNMT in cancer therapy: Role of recombinant protein screening"
**作者**: Duffy, M.J. et al.
**摘要**: 通过重组RNMT高通量筛选小分子抑制剂，发现其抑制可降低癌基因mRNA稳定性，并在乳腺癌模型中验证其抗肿瘤效果。
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提示：实际研究中建议通过PubMed或Web of Science以“RNMT recombinant protein”为关键词检索最新文献，并优先选择结构生物学、酶学或疾病模型相关的高影响力期刊论文。
RNMT (RNA guanine-7 methyltransferase) is a critical enzyme involved in the methylation of the 5' cap structure of eukaryotic mRNA. This cap, consisting of a 7-methylguanosine (m7G) linked to the mRNA via a 5'-5' triphosphate bridge, is essential for mRNA stability, nuclear export, and efficient translation. RNMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to the guanine at the N7 position, completing the final step of cap formation. The enzyme operates in conjunction with the cap-binding complex (CBC) and interacts with RNA polymerase II during transcription initiation, linking mRNA capping to transcriptional regulation.
Structurally, RNMT contains a catalytic domain conserved across methyltransferases and a unique N-terminal domain that mediates interactions with regulatory subunits, such as RAM (RNMT-activating miniprotein). RAM binding enhances RNMT’s catalytic activity, suggesting a regulatory mechanism for cap methylation. Dysregulation of RNMT has been implicated in diseases, including cancer, where aberrant mRNA capping may drive oncogenic protein synthesis. For instance, elevated RNMT expression correlates with poor prognosis in certain malignancies.
Recombinant RNMT proteins are produced using heterologous expression systems (e.g., E. coli or mammalian cells) to study enzymatic mechanisms, screen inhibitors, or explore therapeutic targets. These proteins retain methyltransferase activity when purified and are often used in biochemical assays to dissect capping dynamics or validate drug candidates. Recent studies also employ RNMT mutants or truncations to map functional domains or engineer variants with altered activity. As mRNA-based therapies (e.g., vaccines, gene editing) advance, understanding RNMT’s role in cap quality control remains pivotal for optimizing synthetic mRNA design and cellular delivery systems.
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