| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MTHFS |
| Uniprot No | P49914 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-203aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAAAAVSSAKRSLRGELKQRLRAMSAEERL RQSRVLSQKVIAHSEYQKSKRISIFLSMQDEIETEEIIKDIFQRGKICFI PRYRFQSNHMDMVRIESPEEISLLPKTSWNIPQPGEGDVREEALSTGGLD LIFMPGLGFDKHGNRLGRGKGYYDAYLKRCLQHQEVKPYTLALAFKEQIC LQVPVNENDMKVDEVLYEDSSTA |
| 预测分子量 | 25 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MTHFS重组蛋白的3篇示例参考文献(内容基于研究领域常见方向，实际引用时请核实文献真实性)：
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1. **文献名称**: *"Cloning, expression, and characterization of human MTHFS in Escherichia coli"*
**作者**: Tudor, C. et al. (2008)
**摘要**: 该研究成功克隆了人源MTHFS基因，并在大肠杆菌中实现高效可溶性表达。通过亲和层析纯化获得重组蛋白，酶活实验表明其催化5-甲酰四氢叶酸转化为5.10-亚甲基四氢叶酸的活性，为后续功能研究奠定基础。
2. **文献名称**: *"Kinetic analysis of recombinant MTHFS and its role in folate metabolism"*
**作者**: Smith, J.L. & Stover, P.J. (2012)
**摘要**: 研究利用重组MTHFS蛋白进行酶动力学分析，揭示其Km和Vmax值，并证明其在叶酸代谢循环中维持5-甲酰四氢叶酸稳态的关键作用。通过突变实验发现特定氨基酸残基对酶活性的影响。
3. **文献名称**: *"Structural insights into MTHFS catalysis via X-ray crystallography of the recombinant enzyme"*
**作者**: Johnson, K.A. et al. (2015)
**摘要**: 通过X射线晶体学解析重组MTHFS蛋白的三维结构，阐明了其底物结合位点及催化机制。研究还利用定点突变验证了ATP依赖的环化反应中关键结构域的功能。
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**提示**：若需真实文献，建议在PubMed或Google Scholar检索关键词“MTHFS recombinant protein”或“5-formyltetrahydrofolate cycloligase expression”，并筛选近年高影响力论文。
**Background of MTHFS Recombinant Protein**
Methylenetetrahydrofolate synthetase (MTHFS) is a critical enzyme in folate-mediated one-carbon metabolism, a pathway essential for nucleotide synthesis, methylation reactions, and amino acid homeostasis. Specifically, MTHFS catalyzes the ATP-dependent conversion of 5-formyltetrahydrofolate (5-formyl-THF) to 5.10-methenyl-THF, a reaction that helps regulate the balance of folate derivatives required for cellular proliferation and function. Dysregulation of MTHFS activity has been implicated in metabolic disorders, cancer, and developmental defects, underscoring its biological significance.
Recombinant MTHFS protein is engineered using molecular cloning techniques to enable large-scale production and functional studies. The gene encoding MTHFS is inserted into expression vectors (e.g., bacterial, yeast, or mammalian systems), allowing heterologous expression in hosts like *E. coli* or HEK293 cells. This approach ensures high purity and yield, facilitating biochemical characterization, structural analysis (e.g., X-ray crystallography), and inhibitor screening. Recombinant MTHFS retains enzymatic activity, making it invaluable for investigating folate metabolism mechanisms, substrate specificity, and the impact of genetic mutations.
Interest in MTHFS also stems from its potential as a therapeutic target. For instance, elevated MTHFS expression in certain cancers correlates with increased demand for one-carbon units to support rapid cell division. Conversely, MTHFS deficiency disrupts mitochondrial folate cycling, linked to neurological and cardiovascular pathologies. Recombinant variants, including tagged or mutated forms, aid in developing targeted therapies or diagnostic tools.
Overall, recombinant MTHFS serves as a vital tool for advancing our understanding of folate biology and its implications in disease, bridging gaps between metabolic biochemistry and clinical research.
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