| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MDH1 |
| Uniprot No | P40925 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-334aa |
| 氨基酸序列 | MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVL DGVLMELQDCALPLLKDVIATDKEDVAFKDLDVAILVGSMPRREGMERKD LLKANVKIFKSQGAALDKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKE NFSCLTRLDHNRAKAQIALKLGVTANDVKNVIIWGNHSSTQYPDVNHAKV KLQGKEVGVYEALKDDSWLKGEFVTTVQQRGAAVIKARKLSSAMSAAKAI CDHVRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFV EGLPINDFSREKMDLTAKELTEEKESAFEFLSSALEHHHHHH |
| 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MDH1重组蛋白的3篇参考文献示例(文献信息为虚拟示例，仅供参考)：
1. **文献名称**：*Heterologous Expression and Characterization of Recombinant Human MDH1 in E. coli*
**作者**：Smith J. et al.
**摘要**：该研究报道了人源MDH1基因在大肠杆菌中的重组表达及纯化，通过优化表达条件获得高活性可溶性蛋白，并分析了其酶动力学参数。
2. **文献名称**：*Structural Insights into the Catalytic Mechanism of MDH1 via Crystallography*
**作者**：Lee S. et al.
**摘要**：利用重组表达的MDH1蛋白进行晶体结构解析，揭示了其底物结合位点和催化活性中心的关键氨基酸残基，为酶功能改造提供结构基础。
3. **文献名称**：*Recombinant MDH1 as a Biomarker for Cancer Metabolism Studies*
**作者**：Zhang Y. et al.
**摘要**：研究通过重组MDH1蛋白验证其在肿瘤细胞线粒体代谢中的调控作用，发现其酶活性与癌细胞增殖和糖酵解途径密切相关。
4. **文献名称**：*Optimization of MDH1 Protein Production in Insect Cells for Drug Screening*
**作者**：Chen R. et al.
**摘要**：开发了基于昆虫细胞表达系统的MDH1重组蛋白规模化制备方法，并应用于高通量药物筛选，鉴定出新型小分子抑制剂。
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注：以上文献为示例，实际研究中建议通过PubMed或Web of Science检索真实文献。
Malate dehydrogenase 1 (MDH1) is a key metabolic enzyme that catalyzes the reversible oxidation of malate to oxaloacetate in the citric acid cycle, linking carbohydrate metabolism with cellular energy production. As a NAD⁺-dependent enzyme, MDH1 primarily localizes to the mitochondrial matrix, where it facilitates the malate-aspartate shuttle—a critical pathway for transferring reducing equivalents (NADH) across mitochondrial membranes to support ATP synthesis. Dysregulation of MDH1 has been implicated in metabolic disorders, cancer progression, and neurodegenerative diseases, making it a target for therapeutic and diagnostic research.
Recombinant MDH1 protein is engineered through molecular cloning techniques, often expressed in bacterial (e.g., *E. coli*), yeast, or mammalian cell systems to ensure high purity and functional activity. Its production involves inserting the human *MDH1* gene into expression vectors, followed by fermentation and affinity chromatography purification. Recombinant technology allows for modifications such as tagging (e.g., His-tag) to simplify isolation or enable structural studies.
Biochemically, MDH1 functions as a homodimer, with each subunit containing a Rossmann fold for NAD⁺ cofactor binding and a substrate-specific active site. Recombinant MDH1 is widely used to study enzyme kinetics, metabolic flux analysis, and redox balance in vitro. It also serves as a tool for drug screening targeting metabolic diseases or cancer, where altered MDH1 activity influences tumor growth via ATP synthesis or antioxidant pathways. Additionally, it aids in developing diagnostic assays for conditions linked to mitochondrial dysfunction. Structural analysis of recombinant MDH1 provides insights into mutation effects and mechanisms underlying genetic metabolic disorders.
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