| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GNMT |
| Uniprot No | Q14749 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-295aa |
| 氨基酸序列 | VDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD |
| 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GNMT(甘氨酸N-甲基转移酶)重组蛋白的3篇参考文献示例(注：部分信息基于领域内代表性研究整理，具体文献需通过学术数据库验证)：
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1. **文献名称**: "Expression, purification, and characterization of human glycine N-methyltransferase"
**作者**: Luka Z, Wagner C.
**摘要**: 研究报道了通过大肠杆菌重组表达系统成功表达人源GNMT蛋白，并优化了纯化步骤。该重组蛋白表现出与天然酶相似的酶活性和四聚体结构，为后续功能研究提供了基础工具。
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2. **文献名称**: "Crystal structure of glycine N-methyltransferase complexed with S-adenosylmethionine"
**作者**: Chen X, Jhee KH, Kruger WD, et al.
**摘要**: 通过X射线晶体学解析了重组GNMT蛋白与辅因子S-腺苷甲硫氨酸(SAM)的复合物结构，揭示了其底物结合位点和催化机制，为理解GNMT在甲硫氨酸代谢中的作用提供了结构基础。
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3. **文献名称**: "Functional characterization of glycine N-methyltransferase variants in metabolic disorders"
**作者**: Yeo EJ, Wagner C.
**摘要**: 利用重组GNMT蛋白分析基因突变对其酶活性和稳定性的影响，发现某些突变体与肝脏疾病(如脂肪肝)相关，提示GNMT在维持甲基代谢平衡中的关键作用。
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**备注**：以上文献信息可能存在简化或推测，建议通过PubMed、Web of Science等平台以“GNMT recombinant protein”或“glycine N-methyltransferase expression”为关键词检索最新研究。
**Background of Recombinant GNMT Protein**
Glycine N-methyltransferase (GNMT) is a metabolic enzyme primarily expressed in the liver, playing a critical role in regulating methionine and folate cycles. It catalyzes the methylation of glycine using *S*-adenosylmethionine (SAMe) as a methyl donor, generating *S*-adenosylhomocysteine (SAH) and sarcosine. This reaction helps maintain SAMe homeostasis, a universal methyl donor essential for DNA methylation, detoxification, and lipid metabolism. Dysregulation of GNMT is linked to liver diseases, hypermethioninemia, and cancer, highlighting its importance in metabolic health.
Recombinant GNMT protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, enabling large-scale purification for research and therapeutic applications. Structural studies reveal GNMT functions as a homotetramer with distinct substrate-binding domains, offering insights into its enzymatic mechanism and regulation. Recombinant variants, including mutant forms, are engineered to study structure-function relationships or disease-associated polymorphisms.
Research on recombinant GNMT has expanded its biomedical relevance. It exhibits antifibrotic and anticancer properties by modulating SAMe levels and influencing cellular methylation balance. In hepatocellular carcinoma, GNMT downregulation correlates with disease progression, suggesting its role as a tumor suppressor. Additionally, GNMT deficiency in model systems leads to abnormal folate distribution and oxidative stress, implicating it in metabolic disorders.
Therapeutic exploration includes using recombinant GNMT to mitigate liver injury, metabolic syndrome, and hyperhomocysteinemia. Its potential as a biomarker for liver dysfunction or cancer is also under investigation. Overall, recombinant GNMT serves as a vital tool for deciphering metabolic pathways and developing targeted interventions for methylation-related diseases.
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