| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MTR |
| Uniprot No | Q99707 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1094-1203aa |
| 氨基酸序列 | RDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHE RVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLA DIEQSTGIRL |
| 预测分子量 | 38 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. |
以下为示例性参考文献，供学术写作格式参考(建议通过PubMed/Google Scholar核实最新文献)：
1. **标题**：Expression and Purification of Recombinant Human Methionine Synthase Reductase (MTRR) in E. coli
**作者**：Smith JL, et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化人源MTR重组蛋白，优化了诱导条件与亲和层析步骤，获得高活性蛋白用于酶动力学分析。
2. **标题**：Structural Insights into MTR Protein Function via X-ray Crystallography
**作者**：Chen H, Wang Q.
**摘要**：通过X射线晶体学解析MTR重组蛋白的3D结构，揭示其辅因子结合域构象变化对甲基转移活性的调控机制。
3. **标题**：MTR Deficiency Model: Recombinant Protein Rescue in Cellular Homocysteine Metabolism
**作者**：Gomez-Ramirez M, et al.
**摘要**：利用重组MTR蛋白恢复缺陷型细胞株的同型半胱氨酸代谢功能，证实其在甲基循环中的关键作用及潜在治疗应用。
4. **标题**：High-throughput Screening of MTR Inhibitors Using Fluorescence-based Assay
**作者**：Kim S, et al.
**摘要**：基于重组MTR蛋白开发高通量荧光检测法，筛选小分子抑制剂，为相关代谢疾病药物研发提供新工具。
注：以上为模拟文献条目，实际引用请通过学术数据库检索关键词(如"methionine synthase reductase recombinant"或"MTR protein expression")获取真实文献。
**Background of MTR Recombinant Protein**
The MTR (Methionine Synthase) recombinant protein is a key enzyme involved in one-carbon metabolism, critical for DNA methylation, amino acid synthesis, and cellular detoxification. Originally identified in both prokaryotic and eukaryotic organisms, MTR catalyzes the regeneration of methionine from homocysteine using methyltetrahydrofolate as a methyl donor. This reaction is vitamin B12-dependent, linking folate and methionine cycles essential for nucleotide synthesis and epigenetic regulation.
Recombinant MTR protein is produced via heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*), enabling large-scale purification for research and therapeutic applications. Its recombinant form retains enzymatic activity and structural integrity, making it valuable for studying metabolic disorders, cancer biology, and neurodegenerative diseases linked to folate or vitamin B12 deficiencies. Structural studies of recombinant MTR have elucidated its catalytic mechanisms and interactions with cofactors, aiding drug development targeting metabolic pathways.
Recent advances in protein engineering have improved MTR stability and solubility, addressing challenges like oxidative inactivation. Additionally, recombinant MTR is used in diagnostic assays to measure enzymatic activity in clinical samples, aiding in the diagnosis of inborn errors of metabolism. Its role in maintaining cellular redox balance and supporting rapid cell division underscores its relevance in cancer research, where altered one-carbon metabolism is a hallmark.
Overall, MTR recombinant protein serves as a vital tool in both basic and applied research, bridging molecular biology, biochemistry, and medicine to explore metabolic regulation and therapeutic interventions.
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