| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GAMT |
| Uniprot No | Q14353 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-236aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSAPSATPIFAPGENCSPAWGAAPAAYDAA DTHLRILGKPVMERWETPYMHALAAAASSKGGRVLEVGFGMAIAASKVQE APIDEHWIIECNDGVFQRLRDWAPRQTHKVIPLKGLWEDVAPTLPDGHFD GILYDTYPLSEETWHTHQFNFIKNHAFRLLKPGGVLTYCNLTSWGELMKS KYSDITIMFEETQVPALLEAGFRRENIRTEVMALVPPADCRYYAFPQMIT PLVTKGLEHH HHHH |
| 预测分子量 | 30 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3-4篇关于 **GAMT(胍基乙酸N-甲基转移酶)重组蛋白** 的模拟参考文献示例，涵盖其表达、功能及应用研究：
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1. **标题**：*"Heterologous Expression and Characterization of Recombinant Guanidinoacetate N-Methyltransferase in Escherichia coli"*
**作者**：Smith J, et al.
**摘要**：本研究成功将人源GAMT基因克隆至大肠杆菌表达系统，通过优化诱导条件获得可溶性重组蛋白。纯化后的GAMT显示出高催化活性，证实其在体外有效催化胍基乙酸转化为肌酸。该研究为大规模制备功能性GAMT提供了基础。
2. **标题**：*"Structural Insights into the Catalytic Mechanism of Recombinant GAMT via X-ray Crystallography"*
**作者**：Zhang L, et al.
**摘要**：通过X射线晶体学解析了重组GAMT蛋白的三维结构(分辨率2.1 Å)，揭示了其底物结合口袋和甲基转移的关键氨基酸残基。突变实验验证了活性位点对酶功能的必要性，为GAMT缺乏症的药物设计提供了结构基础。
3. **标题**：*"Recombinant GAMT Enzyme Replacement Therapy in a Murine Model of GAMT Deficiency"*
**作者**：Brown K, et al.
**摘要**：在GAMT缺陷小鼠模型中，系统性注射重组人GAMT蛋白显著降低了血浆胍基乙酸水平并恢复了脑肌酸含量，改善了神经功能。研究表明重组GAMT具有潜在治疗遗传性代谢疾病的应用前景。
4. **标题**：*"Optimization of Recombinant GAMT Production in Pichia pastoris for Biotechnological Applications"*
**作者**：Lee S, et al.
**摘要**：利用毕赤酵母高效分泌表达重组GAMT，通过发酵工艺优化使产量提高5倍。纯化蛋白在工业级肌酸合成中表现出稳定催化效率，为生物法生产肌酸提供了新策略。
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**说明**：以上文献为模拟内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。若需具体文献，可提供更详细的研究方向或年份范围进一步筛选。
Guanidinoacetate N-methyltransferase (GAMT) is a critical enzyme in cellular energy metabolism, primarily involved in the biosynthesis of creatine, a molecule essential for ATP regeneration in high-energy-demand tissues such as skeletal muscle, brain, and heart. GAMT catalyzes the final step of creatine synthesis by transferring a methyl group from S-adenosylmethionine (SAM) to guanidinoacetate (GAA), forming creatine and S-adenosylhomocysteine (SAH). This process occurs predominantly in the liver and kidneys, after which creatine is transported to target tissues via the bloodstream.
Deficiencies in GAMT activity due to genetic mutations lead to GAMT deficiency (GAMTD), a rare autosomal recessive disorder classified under cerebral creatine deficiency syndromes (CCDS). Patients with GAMTD exhibit severe neurological symptoms, including intellectual disability, seizures, and movement disorders, stemming from creatine depletion and toxic accumulation of GAA. Early diagnosis and intervention, such as creatine supplementation and dietary modifications, are crucial to mitigate symptoms.
Recombinant GAMT protein, produced through genetic engineering in heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells), enables detailed study of its structure, function, and interaction with substrates or inhibitors. This technology facilitates high-yield, purified enzyme preparations for biochemical assays, drug screening, and structural studies (e.g., X-ray crystallography). Furthermore, recombinant GAMT holds therapeutic potential in enzyme replacement strategies for GAMTD, though challenges like delivery to target tissues remain. Research also explores its role in broader metabolic contexts, including SAM-dependent methylation pathways and links to other disorders. Advances in protein engineering and gene therapy may expand its biomedical applications in the future.
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