| 纯度 | >95%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | mdh |
| Uniprot No | P61889 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-312aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMKVAVL GAAGGIGQAL ALLLKTQLPS GSELSLYDIA PVTPGVAVDL SHIPTAVKIK GFSGEDATPA LEGADVVLIS AGVARKPGMD RSDLFNVNAG IVKNLVQQVA KTCPKACIGI ITNPVNTTVA IAAEVLKKAG VYDKNKLFGV TTLDIIRSNT FVAELKGKQP GEVEVPVIGG HSGVTILPLL SQVPGVSFTE QEVADLTKRI QNAGTEVVEA KAGGGSATLS MGQAAARFGL SLVRALQGEQ GVVECAYVEG DGQYARFFSQ PLLLGKNGVE ERKSIGTLSA FEQNALEGML DTLKKDIALG EEFVNK |
| 预测分子量 | 35 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MDH（苹果酸脱氢酶）重组蛋白的3篇代表性文献摘要概括（注：文献为示例，非真实存在）：
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1. **标题**：*Cloning and expression of thermostable malate dehydrogenase from Thermococcus kodakarensis in E. coli* **作者**：Tanaka K. et al. **摘要**：研究报道了一种来自超嗜热古菌的MDH基因在大肠杆菌中的高效表达及纯化，重组酶在80°C下仍保持活性，为高温工业催化提供了潜在工具。
2. **标题**：*Optimization of recombinant malate dehydrogenase production in Pichia pastoris for biocatalytic applications* **作者**：Müller S. et al. **摘要**：通过优化毕赤酵母表达系统，显著提高了重组MDH的产量，并验证其在体外催化苹果酸合成中的高效性，为规模化生产奠定基础。
3. **标题**：*Engineering malate dehydrogenase for enhanced NADH regeneration in metabolic pathways* **作者**：Chen L. et al. **摘要**：通过定点突变改造MDH的辅酶结合位点，提高了其对NADH的再生效率，证明其在细胞工厂构建中提升代谢通量的潜力。
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如需真实文献，建议通过PubMed或Web of Science检索关键词“recombinant malate dehydrogenase expression”或“MDH protein engineering”。
Malate dehydrogenase (MDH) is a ubiquitously conserved enzyme central to cellular metabolism, catalyzing the reversible oxidation of malate to oxaloacetate using NAD+/NADH as a cofactor. It exists in two primary isoforms: mitochondrial MDH (mMDH), which participates in the tricarboxylic acid (TCA) cycle, and cytoplasmic MDH (cMDH), involved in the malate-aspartate shuttle and redox balance. Due to its critical role in energy production and metabolic pathways, MDH has become a focal point in biochemical research, particularly in studies related to metabolic disorders, cancer, and microbial physiology.
Recombinant MDH technology emerged with advancements in genetic engineering, enabling large-scale production of the enzyme for research and industrial applications. By cloning MDH genes into expression vectors (e.g., E. coli, yeast, or mammalian systems), scientists produce purified, high-activity MDH with customizable modifications. This approach overcomes limitations of native protein extraction, such as low yield and contamination risks. Affinity tags (e.g., His-tags) and optimized purification protocols ensure enzyme homogeneity and stability.
Recombinant MDH is widely used in enzymology to study catalytic mechanisms, allosteric regulation, and structural dynamics via X-ray crystallography. Industrially, it serves in biosensors for metabolite detection, biofuel production through NADH regeneration systems, and pharmaceutical synthesis. Recent studies explore engineered MDH variants for enhanced thermal stability or substrate specificity, relevant to biomanufacturing and therapeutic development. Additionally, MDH's association with tumor metabolism has spurred interest in its potential as a cancer biomarker or drug target. The accessibility of recombinant MDH continues to drive interdisciplinary innovations in biochemistry, synthetic biology, and precision medicine.
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