| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | N6AMT1 |
| Uniprot No | Q9Y5N5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-214aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMNIRNARPEDLMNMQHCNLLCLPENYQMKY YFYHGLSWPQLSYIAEDE NGKIVGYVLAKMEEDPDDVPHGHITSLAVK RSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKSNRAALHLYS NTL NFQISEVEPKYYADGEDAYAMKRDLTQMADELRRHLELKEKGRHVVLGAI ENKVESKGNSPPSSGEACREEK GLAAEDSGGDSKDLSEVSETTESTDV KDSSEASDSAS |
| 预测分子量 | 25 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N6AMT1重组蛋白的示例参考文献(内容为模拟示例，具体文献需通过学术数据库验证)：
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1. **标题**: *"Recombinant expression and functional characterization of human N6AMT1 in arsenic methylation"*
**作者**: Thomas R, et al.
**摘要**: 研究报道了在大肠杆菌中重组表达人源N6AMT1蛋白，并验证其在体外催化砷甲基化的功能，揭示了其在砷代谢解毒中的潜在作用。
2. **标题**: *"Structural insights into N6AMT1 substrate specificity using crystallography and site-directed mutagenesis"*
**作者**: Chen L, et al.
**摘要**: 通过重组表达并纯化N6AMT1蛋白，结合X射线晶体学解析其三维结构，阐明了底物结合的关键氨基酸残基及其催化机制。
3. **标题**: *"Development of a mammalian cell-based system for high-yield production of bioactive N6AMT1"*
**作者**: Wang Y, et al.
**摘要**: 开发了基于HEK293细胞的重组N6AMT1蛋白表达系统，优化纯化工艺后获得高活性蛋白，用于后续酶动力学及抑制剂筛选研究。
4. **标题**: *"N6AMT1 recombinant protein exhibits methyltransferase activity toward histone peptides in vitro"*
**作者**: Smith J, et al.
**摘要**: 研究利用重组N6AMT1蛋白进行体外甲基转移实验，发现其对组蛋白H3特定赖氨酸残基的修饰能力，提示可能的表观遗传调控功能。
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建议通过 **PubMed** 或 **Web of Science** 检索最新文献，关键词：**N6AMT1 recombinant protein** / **N6AMT1 expression**。
N6AMT1 (N-6 adenine-specific DNA methyltransferase 1), also known as MTQ2 or HENMT1. is a conserved S-adenosylmethionine (SAM)-dependent methyltransferase that plays roles in epigenetic regulation and xenobiotic metabolism. Initially identified for its homology to bacterial DNA methyltransferases, it was later found to catalyze methyl group transfer to adenine residues in specific nucleic acid contexts, though its primary biological substrates remain under investigation. Notably, N6AMT1 gained attention for its ability to methylate inorganic arsenic metabolites, converting monomethylarsonous acid (MMAIII) to dimethylarsonic acid (DMAV), a process potentially linked to arsenic detoxification or toxicity amplification depending on cellular context.
The recombinant N6AMT1 protein, typically produced in E. coli or mammalian expression systems, retains the conserved catalytic domain structure featuring a SAM-binding motif and target recognition regions. Structural studies reveal a Rossmann-like fold characteristic of class I methyltransferases. Its 278-amino acid sequence (≈31 kDa) includes conserved motifs (I, post-I, II, III) essential for cofactor binding and catalytic activity.
Research applications focus on its dual roles: 1) In epigenetics, potential involvement in DNA/RNA modification pathways influencing gene regulation; 2) In toxicology, modulating arsenic metabolism and cellular responses to environmental toxins. Aberrant N6AMT1 expression has been associated with various cancers, with both tumor-suppressive and oncogenic effects reported depending on cancer type. Recent studies suggest additional functions in spermidine metabolism and chemotherapy resistance mechanisms. The recombinant protein serves as a critical tool for elucidating its enzymatic specificity, developing arsenic biosensors, and screening potential inhibitors for therapeutic applications. Ongoing research aims to clarify its endogenous substrates and resolve controversies regarding its primary biological functions across different tissue contexts.
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