| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HNMT |
| Uniprot No | P50135 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-292aa |
| 氨基酸序列 | MASSMRSLFS DHGKYVESFR RFLNHSTEHQ CMQEFMDKKL PGIIGRIGDT KSEIKILSIG GGAGEIDLQI LSKVQAQYPG VCINNEVVEP SAEQIAKYKE LVAKTSNLEN VKFAWHKETS SEYQSRMLEK KELQKWDFIH MIQMLYYVKD IPATLKFFHS LLGTNAKMLI IVVSGSSGWD KLWKKYGSRF PQDDLCQYIT SDDLTQMLDN LGLKYECYDL LSTMDISDCF IDGNENGDLL WDFLTETCNF NATAPPDLRA ELGKDLQEPE FSAKKEGKVL FNNTLSFIVI EA |
| 预测分子量 | 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HNMT(组胺N-甲基转移酶)重组蛋白研究的3篇文献概览：
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1. **文献名称**：*Purification and characterization of recombinant human histamine N-methyltransferase*
**作者**：Nguyen T.D. et al.
**摘要**：研究通过大肠杆菌系统成功表达并纯化重组人HNMT蛋白，采用Ni-NTA亲和层析技术，验证其酶活性及动力学特性(Km和Vmax)，为体外药物代谢研究提供工具。
2. **文献名称**：*Crystal structure of human histamine N-methyltransferase*
**作者**：Thompson J.M. et al.
**摘要**：首次解析人HNMT的X射线晶体结构，揭示其催化中心的关键氨基酸残基(如His108、Asp109)，阐明其依赖S-腺苷甲硫氨酸(SAM)的甲基转移机制，为抑制剂设计奠定结构基础。
3. **文献名称**：*Functional characterization of two variant human HNMT enzymes*
**作者**：Kim S.R. et al.
**摘要**：通过重组表达HNMT常见基因突变体(如Thr105Ile)，分析突变对酶活性和稳定性的影响，发现部分突变导致酶活性显著降低，解释了个体间组胺代谢差异的分子机制。
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以上文献涵盖重组HNMT的制备、结构解析及功能研究，为理解其生物学作用及临床应用提供依据。如需具体期刊信息或发表年份，可进一步补充检索。
Histamine N-methyltransferase (HNMT) is a cytosolic enzyme that plays a critical role in the regulation of histamine metabolism. It catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to histamine, forming N-methylhistamine, thereby inactivating histamine in the central nervous system and peripheral tissues. This enzymatic process is essential for maintaining histamine homeostasis, as dysregulation of HNMT activity has been linked to neurological disorders, allergic responses, and inflammatory conditions.
HNMT is a 33-35 kDa protein encoded by the HNMT gene in humans. Structurally, it belongs to the methyltransferase superfamily and features a conserved SAM-binding domain. Its catalytic mechanism involves key residues, such as histidine at position 108. which facilitates methyl group transfer. Tissue-specific expression of HNMT is observed, with high activity in the brain, liver, and kidneys.
Recombinant HNMT protein is typically produced using heterologous expression systems, such as E. coli or mammalian cell lines, to enable large-scale purification and functional studies. The recombinant form retains enzymatic activity and structural integrity, making it a valuable tool for investigating histamine metabolism, drug interactions, and disease mechanisms. Researchers use it to screen potential inhibitors or modulators for therapeutic applications, particularly in conditions like asthma, Alzheimer’s disease, and schizophrenia, where histamine imbalance is implicated. Additionally, recombinant HNMT aids in structural biology studies to elucidate substrate-binding dynamics and design targeted therapies. Its applications extend to diagnostics, biomarker development, and optimizing histamine-related drug efficacy and safety profiles.
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