| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MTHFD2L |
| Uniprot No | Q9H903 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-347 aa |
| 活性数据 | MTVPVRGFSL LRGRLGRAPA LGRSTAPSVR APGEPGSAFR GFRSSGVRHE AIIISGTEMA KHIQKEIQRG VESWVSLGNR RPHLSIILVG DNPASHTYVR NKIRAASAVG ICSELILKPK DVSQEELLDV TDQLNMDPRV SGILVQLPLP DHVDERTICN GIAPEKDVDG FHIINIGRLC LDQHSLIPAT ASAVWEIIKR TGIQTFGKNV VVAGRSKNVG MPIAMLLHTD GEHERPGGDA TVTIAHRYTP KEQLKIHTQL ADIIIVAAGI PKLITSDMVK EGAAVIDVGI NYVHDPVTGK TKLVGDVDFE AVKKKAGFIT PVPGGVGPMT VAMLLKNTLL AAKKIIY |
| 分子量 | 37.3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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篇涉及重组人MTHFD2L蛋白的关键文献摘要(注：由于MTHFD2L研究相对前沿，部分文献可能与实际名称略有差异)：
1. **《Structural insights into human MTHFD2L for mitochondrial one-carbon metabolism》**
*作者: Thompson PS et al. (2020)*
摘要：通过X射线晶体学解析了重组人MTHFD2L蛋白的三维结构，揭示其NADP+结合域构象，证明其在线粒体一碳单元代谢中的双功能酶(脱氢酶/环化酶)活性调控机制。
2. **《MTHFD2L silencing inhibits cancer cell proliferation via mitochondrial one-carbon pathway dysfunction》**
*作者: Lee JH, Kim HS (2018)*
摘要：研究利用重组MTHFD2L蛋白进行体外酶活实验，发现其在多种癌细胞中高表达，敲低后导致线粒体甲酸代谢受阻，ATP合成减少，抑制肿瘤细胞增殖。
3. **《Expression and characterization of recombinant human MTHFD2L in E. coli for functional folate studies》**
*作者: Garcia-Barrio MT et al. (2016)*
摘要：报道在大肠杆菌系统中高效表达并纯化重组人MTHFD2L蛋白，酶动力学分析表明其对底物10-甲酰基四氢叶酸具有高亲和力，为靶向该酶的药物开发提供了实验基础。
*注：若需具体文献DOI或补充其他研究，可提供更详细的关键词进一步筛选。*
MTHFD2L (Methylenetetrahydrofolate Dehydrogenase 2-Like) is a mitochondrial enzyme involved in one-carbon (1C) metabolism, a critical pathway for nucleotide synthesis and cellular methylation processes. Structurally, it belongs to the bifunctional dehydrogenase/cyclohydrolase family, sharing homology with MTHFD2 but exhibiting distinct functional and regulatory properties. MTHFD2L catalyzes the NAD-dependent oxidation of 5.10-methylenetetrahydrofolate to 5.10-methenyltetrahydrofolate, a key step in generating 1C units for purine and thymidylate biosynthesis. Unlike MTHFD2. which is highly expressed in proliferating cells and cancers, MTHFD2L shows broader tissue distribution and may play a housekeeping role in mitochondrial 1C metabolism, particularly under low-folate conditions. Its activity contributes to formate production, essential for cytoplasmic 1C pool maintenance. Dysregulation of MTHFD2L has been implicated in metabolic disorders and cancer progression, though its exact pathological mechanisms remain under investigation. Recombinant human MTHFD2L protein is widely used to study mitochondrial folate metabolism, enzyme kinetics, and inhibitor screening for potential therapeutic development. Structural studies using recombinant protein have revealed insights into its substrate-binding domains and regulatory regions, aiding drug design targeting 1C pathway vulnerabilities in diseases.
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