| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | INMT |
| Uniprot No | O95050 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-263aa |
| 氨基酸序列 | MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLIDIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGNSGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAALCNLASLLKPGGHLVTTVTLRLPSYMVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQSYSVTNAANNGVCFIVARKKPGP |
| 预测分子量 | 44.9 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INMT重组蛋白的3篇参考文献及其摘要概括：
1. **"Expression and characterization of recombinant human indolethylamine N-methyltransferase"**
- **作者**: Thompson, M.A., Weinshilboum, R.M.
- **摘要**: 该研究报道了人源INMT基因在大肠杆菌中的重组表达，纯化后酶活性分析表明其可催化色胺类底物的甲基化反应，为后续功能研究奠定基础。
2. **"Molecular cloning and functional expression of human indolethylamine N-methyltransferase"**
- **作者**: Cozzi, N.V., et al.
- **摘要**: 通过克隆人INMT cDNA并在哺乳动物细胞中重组表达，证实其催化N-甲基转移活性，并揭示了底物特异性及酶动力学特征。
3. **"Purification and biochemical characterization of recombinant rabbit INMT"**
- **作者**: Wu, H., et al.
- **摘要**: 优化了兔源INMT重组蛋白的纯化流程，分析了pH和温度对酶活性的影响，并鉴定了多种天然及合成抑制剂的作用效果。
4. **"Structural insights into the catalytic mechanism of INMT through X-ray crystallography"**
- **作者**: Zhang, Y., et al.
- **摘要**: 解析了重组表达的人INMT蛋白的晶体结构，阐明了其甲基供体(SAM)结合位点及底物催化机制，为靶向药物设计提供结构基础。
(注：上述文献信息为示例性概括，实际引用时请核对真实文献。)
**Background of INMT Recombinant Protein**
Indolethylamine *N*-methyltransferase (INMT) is an enzyme that catalyzes the transfer of methyl groups from *S*-adenosylmethionine (SAM) to endogenous indolethylamine substrates, including tryptamine and dimethyltryptamine (DMT). This enzyme plays a role in the biosynthesis of methylated neurotransmitters and psychoactive compounds, potentially influencing neurological and physiological processes. INMT is expressed in various tissues, including the brain, lungs, and adrenal glands, though its precise biological functions remain under investigation.
Recombinant INMT protein is produced using genetic engineering techniques, typically by cloning the INMT gene into expression vectors (e.g., *E. coli* or mammalian systems) to enable large-scale production. Purification methods like affinity chromatography (e.g., His-tag systems) ensure high purity and activity. Recombinant INMT retains enzymatic functionality, allowing researchers to study its substrate specificity, kinetic properties, and regulatory mechanisms *in vitro*.
Interest in INMT stems from its potential link to neuropsychiatric disorders, such as schizophrenia, and its role in endogenous DMT synthesis, which has been hypothesized to modulate consciousness or immune responses. Additionally, INMT-mediated methylation may influence cancer progression by altering metabolite profiles. Recombinant INMT serves as a critical tool for drug discovery, enabling screening of inhibitors or modulators targeting methylation pathways.
Despite advances, challenges remain in elucidating INMT's physiological relevance, structural dynamics, and interactions with cellular components. Ongoing research leverages recombinant protein technology to address these gaps, offering insights into its therapeutic potential and role in human health.
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