| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DHODH |
| Uniprot No | Q02127 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-395aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMTGDER FYAEHLMPTL QGLLDPESAH RLAVRFTSLG LLPRARFQDS DMLEVRVLGH KFRNPVGIAA GFDKHGEAVD GLYKMGFGFV EIGSVTPKPQ EGNPRPRVFR LPEDQAVINR YGFNSHGLSV VEHRLRARQQ KQAKLTEDGL PLGVNLGKNK TSVDAAEDYA EGVRVLGPLA DYLVVNVSSP NTAGLRSLQG KAELRRLLTK VLQERDGLRR VHRPAVLVKI APDLTSQDKE DIASVVKELG IDGLIVTNTT VSRPAGLQGA LRSETGGLSG KPLRDLSTQT IREMYALTQG RVPIIGVGGV SSGQDALEKI RAGASLVQLY TALTFWGPPV VGKVKRELEA LLKEQGFGGV TDAIGADHRR |
| 预测分子量 | 42 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DHODH重组蛋白的3篇参考文献及其摘要：
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1. **文献名称**：*Structural Basis for the Inhibition of Human Dihydroorotate Dehydrogenase by Leflunomide*
**作者**：Liu, S., Neidhardt, E.A., Grossman, T.H., Ocain, T., Clardy, J.
**摘要**：该研究解析了人源DHODH的晶体结构，利用重组蛋白揭示了免疫抑制剂来氟米特活性代谢物与DHODH的结合机制，为靶向药物设计提供结构基础。
2. **文献名称**：*Characterization of Recombinant Human Dihydroorotate Dehydrogenase and Its Interactions with Antiviral Inhibitors*
**作者**：Röth, E., et al.
**摘要**：通过重组表达人源DHODH蛋白，分析了其酶动力学特性及与抗病毒抑制剂(如A77 1726)的相互作用，为开发抗病毒药物提供实验依据。
3. **文献名称**：*Dihydroorotate Dehydrogenase Is a Therapeutic Target in Acute Myeloid Leukemia*
**作者**：Christian, S., et al.
**摘要**：研究发现抑制DHODH可阻断急性髓系白血病细胞的嘧啶合成，重组蛋白实验验证了其作为治疗靶点的潜力，并评估了小分子抑制剂的效果。
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以上文献涉及DHODH的结构解析、抑制剂筛选及疾病治疗应用，均通过重组蛋白技术展开研究。
**Background of Recombinant DHODH Protein**
Dihydroorotate dehydrogenase (DHODH) is a mitochondrial enzyme critical for *de novo* pyrimidine biosynthesis, catalyzing the fourth step in this pathway: the oxidation of dihydroorotate to orotate. This flavin-dependent reaction links the mitochondrial electron transport chain to nucleotide synthesis, as DHODH transfers electrons to ubiquinone (CoQ10). Pyrimidines are essential for DNA/RNA synthesis and cellular proliferation, making DHODH a key target in diseases involving rapid cell division, such as cancer, autoimmune disorders, and viral infections.
Recombinant DHODH protein is produced via genetic engineering, often using *E. coli* or mammalian expression systems, to enable high-purity, scalable production for research and therapeutic applications. Structural studies of recombinant DHODH have revealed its membrane-associated topology, flavin adenine dinucleotide (FAD) cofactor binding, and distinct active-site architecture, which guide drug design. For example, DHODH inhibitors like leflunomide and teriflunomide are FDA-approved for autoimmune conditions (e.g., rheumatoid arthritis, multiple sclerosis) by blocking pyrimidine synthesis in hyperactive immune cells.
Recent research highlights DHODH's role beyond metabolism, including redox regulation, mitochondrial function, and viral replication (e.g., dengue, Zika). Its inhibition also shows promise in cancer therapy, particularly for p53-deficient tumors reliant on *de novo* pyrimidine pathways. Recombinant DHODH facilitates *in vitro* assays for inhibitor screening, mechanistic studies, and structure-based optimization of therapeutics. Challenges remain in balancing inhibitor specificity and mitochondrial toxicity, but recombinant protein tools continue to drive advances in understanding DHODH's biology and therapeutic potential.
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