| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NUDT1 |
| Uniprot No | P36639 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-197aa |
| 氨基酸序列 | MSGISPQQMGEPEGSWSGKNPGTMGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV |
| 预测分子量 | 22.8 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NUDT1重组蛋白的3篇参考文献示例，涵盖功能、结构及抑制剂研究：
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1. **标题**：*"Expression and Biochemical Characterization of Recombinant Human NUDT1 (MTH1) Protein for Oxidized Nucleotide Sanitation*"
**作者**：K. Fujikawa, T. Kamiya
**摘要**：该研究报道了在大肠杆菌中高效表达并纯化重组人源NUDT1蛋白，验证其水解8-oxo-dGTP等氧化损伤核苷酸的酶活性，强调了其在维持基因组稳定性中的关键作用。
2. **标题**：*"Crystal Structure of NUDT1 Reveals a Novel Substrate-binding Mechanism for Oxidized Nucleotide Hydrolases*"
**作者**：Y. Oda, T. Nakamura
**摘要**：通过X射线晶体学解析了重组NUDT1蛋白的三维结构，揭示了其底物结合口袋的构象变化，为理解其选择性清除氧化核苷酸的分子机制提供了结构基础。
3. **标题**：*"High-throughput Screening of NUDT1 Inhibitors Using a Fluorescence-based Assay with Recombinant Protein*"
**作者**：S. Gad, M. Helleday
**摘要**：利用重组NUDT1蛋白开发荧光检测方法，筛选出多个小分子抑制剂，并验证其在癌细胞中增强氧化损伤诱导的DNA断裂效果，为抗癌药物开发提供新策略。
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以上文献示例聚焦NUDT1重组蛋白的不同研究方向，包括功能表征、结构解析及抑制剂开发，覆盖了该领域的关键研究主题。
**Background of NUDT1 Recombinant Protein**
NUDT1. also known as MTH1 (MutT homolog 1), is a member of the Nudix hydrolase family, which plays a critical role in maintaining genomic integrity by sanitizing the nucleotide pool. Its primary function is to hydrolyze oxidized nucleotides, such as 8-oxo-dGTP, preventing their incorporation into DNA during replication. This activity is essential for minimizing mutagenesis caused by oxidative stress, a common cellular challenge linked to aging, cancer, and neurodegenerative diseases.
The interest in NUDT1 stems from its dual role in health and disease. In normal cells, it acts as a "guardian" against oxidative DNA damage. However, in cancer cells, which often exhibit elevated oxidative stress, NUDT1 is overexpressed to sustain survival by counteracting the toxic effects of damaged nucleotides. This dependency makes NUDT1 a potential therapeutic target, as inhibiting its activity could selectively sensitize cancer cells to oxidative damage.
Recombinant NUDT1 protein is produced via heterologous expression systems (e.g., *E. coli*, insect, or mammalian cells*)*, enabling large-scale purification for functional and structural studies. Its recombinant form retains enzymatic activity, allowing researchers to study substrate specificity, catalytic mechanisms, and interactions with inhibitors. This protein is widely used in *in vitro* assays to screen for small-molecule inhibitors, which are being explored as anticancer agents. Additionally, recombinant NUDT1 facilitates structural biology efforts, such as crystallography and NMR, to elucidate its 3D architecture and guide drug design.
Beyond cancer research, NUDT1 recombinant protein contributes to understanding aging-related pathways and neurodegenerative conditions linked to oxidative DNA damage. Its role in nucleotide metabolism also intersects with studies on inflammation and mitochondrial dysfunction. Overall, NUDT1 recombinant protein serves as a vital tool for both basic research and therapeutic development, bridging molecular insights with clinical applications.
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