| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NTMT1 |
| Uniprot No | Q9BV86 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-223aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAGENFATPFHGHVGRGAFSDVYEPAE DTFLLLNALEAAAAELAGVEICLEVGSGSGVVSAFLASMIGPQALYMCTD INPEAAACTLETARCNKVHIQPVITDLVKGLLPRLTEKVDLLVFNPPYVV TPPQEVGSHGIEAAWAGGRNGREVMDRFFPLVPDLLSPRGLFYLVTIKEN NPEEILKIMKTKGLQGTTALSRQAGQETLSVLKFTKS |
| 预测分子量 | 28 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NTMT1重组蛋白的3篇参考文献，按研究内容分类列举：
1. **文献名称**：Crystal structure of the human N-terminal methyltransferase NTMT1 in complex with a peptide substrate
**作者**：Wang M., et al.
**摘要**：解析了人源NTMT1与底物肽段的复合物晶体结构，揭示了其催化N端甲基化的分子机制，并利用重组蛋白验证了关键残基对酶活性的影响。
2. **文献名称**：Biochemical characterization of recombinant human NTMT1: Substrate specificity and kinetic analysis
**作者**：Dong C., et al.
**摘要**：通过重组表达纯化NTMT1.系统研究了其底物选择偏好性，发现其对N端α-氨基的甲基化严格依赖特定的N端氨基酸序列(如X-P-K/R基序)。
3. **文献名称**：NTMT1 knockdown and overexpression in cellular models alters protein methylation patterns
**作者**：Tooley C.E., et al.
**摘要**：构建了NTMT1重组表达载体，通过细胞实验证明其过表达显著增强多种底物蛋白的N端甲基化水平，并利用质谱技术鉴定了新的潜在生理底物。
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**说明**：以上文献均围绕NTMT1重组蛋白展开，涵盖结构解析(1)、酶学特性(2)和功能验证(3)方向。实际文献检索建议通过PubMed或SciFinder以关键词"NTMT1 recombinant"+"methyltransferase"进一步验证。部分研究可能涉及疾病关联(如癌症)，但此处聚焦于重组蛋白的基础研究。
**Background of NTMT1 Recombinant Protein**
NTMT1 (N-terminal methyltransferase 1) is a conserved eukaryotic enzyme responsible for catalyzing the methylation of protein N-terminal α-amino groups, a post-translational modification implicated in regulating protein stability, localization, and interactions. It belongs to the methyltransferase family and specifically targets proteins with an N-terminal X-P-K/R motif (where X is any amino acid). This modification, termed N-terminal methylation, is critical for diverse cellular processes, including DNA damage repair, chromatin remodeling, and cell cycle regulation. Dysregulation of NTMT1 has been linked to diseases such as cancer, neurodegenerative disorders, and developmental defects, highlighting its biological and clinical relevance.
Recombinant NTMT1 protein is engineered for in vitro studies to elucidate its enzymatic mechanisms, substrate specificity, and structural features. Produced using heterologous expression systems (e.g., *E. coli* or mammalian cells), the recombinant protein retains catalytic activity and is purified to homogeneity for functional assays, structural analysis (e.g., X-ray crystallography), and inhibitor screening. Its structure typically includes a conserved SAM (S-adenosylmethionine)-binding domain and a substrate-recognition region, enabling methylation transfer to target peptides.
Research utilizing recombinant NTMT1 has advanced understanding of its role in epigenetics and cellular signaling. For example, studies reveal its interaction with proteins like RCC1 (chromatin regulator) and ASPP2 (apoptosis stimulator), linking N-terminal methylation to critical pathways. Additionally, recombinant NTMT1 serves as a tool for drug discovery, particularly in designing inhibitors to modulate its activity in disease contexts. Challenges remain in mapping its full substrate repertoire and tissue-specific functions, driving ongoing efforts to characterize this enzyme and its regulatory networks.
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