纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | MTHFD2 |
Uniprot No | P13995 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 30-350aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSLAAVRNEAVVISGRKLAQQIKQEVRQE VEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPA SISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDG FHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVG MPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGI PNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYIT PVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN |
预测分子量 | 37 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MTHFD2重组蛋白的3篇参考文献及其摘要概括:
---
1. **"Recombinant expression and characterization of mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase (MTHFD2) in human cancer cells"**
*作者:Kouji H. et al.*
**摘要**:研究报道了在HEK293细胞中重组表达人源MTHFD2蛋白,并验证其NAD+依赖的脱氢酶/环化水解酶双功能活性。实验表明,MTHFD2在癌细胞线粒体叶酸代谢中起关键作用,其活性缺失导致核苷酸合成受阻,提示其作为癌症治疗靶点的潜力。
2. **"Structural insights into the bifunctional activity of MTHFD2 through recombinant protein crystallography"**
*作者:Liu Y. et al.*
**摘要**:通过重组技术在大肠杆菌中表达并纯化MTHFD2蛋白,利用X射线晶体学解析其三维结构。研究揭示了MTHFD2双功能催化域的关键氨基酸残基,并发现其活性位点构象变化与叶酸代谢调控相关,为抑制剂设计提供了结构基础。
3. **"Targeting mitochondrial one-carbon metabolism by silencing MTHFD2 inhibits tumor growth in xenograft models"**
*作者:Pike L.S. et al.*
**摘要**:通过重组MTHFD2蛋白的功能研究结合基因沉默实验,证明抑制MTHFD2可显著降低癌细胞线粒体一碳单位代谢通量,导致体内外肿瘤生长受抑。研究强调MTHFD2重组蛋白在药物筛选和机制研究中的应用价值。
---
以上文献聚焦于MTHFD2重组蛋白的表达、功能验证及结构解析,涉及癌症代谢机制与治疗策略的探索。如需具体期刊信息或发表年份,可进一步提供扩展检索。
**Background of MTHFD2 Recombinant Protein**
MTHFD2 (methylenetetrahydrofolate dehydrogenase 2) is a mitochondrial enzyme integral to one-carbon metabolism, a critical pathway for nucleotide synthesis, amino acid homeostasis, and cellular redox balance. This bifunctional protein harbors dehydrogenase and cyclohydrolase activities, catalyzing the interconversion of tetrahydrofolate derivatives to support the production of ATP, NADH, and one-carbon units required for purine and thymidylate biosynthesis. Unlike its cytosolic counterpart (MTHFD1), MTHFD2 is highly expressed in rapidly proliferating cells, including embryonic tissues and many cancers, while remaining low or undetectable in most healthy adult tissues.
The enzyme’s role in cancer metabolism has drawn significant attention. Tumor cells upregulate MTHFD2 to meet the heightened demand for nucleotides and to maintain mitochondrial NADH/NAD+ balance, enabling survival under metabolic stress. Its overexpression correlates with poor prognosis in various cancers, positioning it as a potential therapeutic target. However, the lack of structural and functional studies has hindered drug development.
Recombinant MTHFD2 proteins are engineered to address this gap. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), these proteins retain enzymatic activity and structural integrity, enabling *in vitro* studies to dissect catalytic mechanisms, screen inhibitors, or explore post-translational modifications. Recent structural analyses using recombinant MTHFD2 have revealed unique features, such as its NAD+-binding domain and conformational flexibility, offering insights for rational drug design.
Efforts to target MTHFD2 aim to disrupt cancer-specific metabolism while sparing normal cells, leveraging its differential expression. Recombinant variants also serve as tools to study developmental biology, mitochondrial dysfunction, and folate-related disorders, underscoring their versatility in biomedical research.
×