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Recombinant Human ME2 protein

  • 中文名: NADP依赖性苹果酶2(ME2)活性蛋白
  • 别    名: ME2;MEL18;RNF110;ZNF144;Polycomb group RING finger protein 2
货号: PA2000-1045
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点ME2
Uniprot No P23368
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间19-584aa
氨基酸序列MLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKIDSYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILCNTRHISDSVFLEAAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAFRYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESASSPPVITE+HHHHHH
预测分子量 64.4 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.

参考文献

以下是关于ME2(线粒体苹果酸酶2)重组蛋白的示例参考文献(注:以下内容为示例,实际文献请通过学术数据库查询):

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1. **文献名称**: "Recombinant Expression and Functional Characterization of Human Mitochondrial Malic Enzyme 2"

**作者**: Lee, J. et al.

**摘要**: 报道了ME2在大肠杆菌中的重组表达及纯化方法,分析了其酶动力学参数,证实重组ME2具有催化苹果酸脱羧的活性,并依赖NAD+辅因子。

2. **文献名称**: "Structural Insights into the Catalytic Mechanism of ME2 via X-ray Crystallography"

**作者**: Smith, R.P. & Gonzalez, A.

**摘要**: 通过X射线晶体学解析了重组ME2的三维结构,揭示了其底物结合位点及催化机制,为针对ME2的抑制剂设计提供了结构基础。

3. **文献名称**: "ME2 Deficiency Alters Cellular Redox State and Promotes Tumor Metastasis"

**作者**: Wang, Y. et al.

**摘要**: 利用重组ME2蛋白及基因敲除模型,证明ME2通过调节NADH/NAD+平衡影响细胞氧化还原状态,进而抑制肿瘤转移。

4. **文献名称**: "Optimization of ME2 Recombinant Protein Production in Pichia pastoris for Industrial Applications"

**作者**: Zhang, H. et al.

**摘要**: 在毕赤酵母系统中优化ME2重组表达条件,实现高产量和高活性ME2制备,为工业级酶生产提供可行方案。

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建议通过 **PubMed**、**Web of Science** 或 **Google Scholar** 检索关键词 "recombinant ME2"、"malic enzyme 2 expression" 获取真实文献。

背景信息

Malic Enzyme 2 (ME2) is a mitochondrial enzyme that plays a critical role in cellular energy metabolism and redox balance. It catalyzes the oxidative decarboxylation of malate to pyruvate, coupled with the reduction of NAD(P)+ to NAD(P)H, linking the tricarboxylic acid (TCA) cycle with glycolysis and lipid synthesis. ME2 has drawn significant attention due to its dual metabolic functions: supporting ATP production through NADH generation and providing precursors for biosynthetic pathways via pyruvate and NADPH. Dysregulation of ME2 has been implicated in various pathological conditions, including cancer, metabolic disorders, and neurodegenerative diseases.

Recombinant ME2 protein production emerged as a key tool for studying its structure-function relationships and therapeutic potential. Using heterologous expression systems like *E. coli*, yeast, or mammalian cell cultures, researchers produce purified ME2 with preserved catalytic activity for biochemical assays. This technology enables detailed investigations into enzyme kinetics, substrate specificity, and allosteric regulation. Notably, ME2 overexpression has been observed in multiple cancers, where it promotes tumor proliferation, metastasis, and chemoresistance by altering metabolic flux and redox homeostasis. Recombinant ME2 facilitates drug discovery efforts, particularly in developing small-molecule inhibitors targeting its oncogenic activity.

Recent studies also explore ME2's role in metabolic syndromes, as its activity influences insulin secretion and lipid metabolism. Structural insights from recombinant protein crystallography have revealed unique conformational changes during catalysis, guiding rational inhibitor design. Challenges remain in optimizing recombinant ME2 stability and mimicking its native mitochondrial environment in vitro. Current research focuses on translating mechanistic insights into therapeutic strategies, positioning recombinant ME2 as both a biological tool and a promising target for precision medicine.

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