| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DUT |
| Uniprot No | P33316 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-252aa |
| 氨基酸序列 | MTPLCPRPALCYHFLTSLLRSAMQNARGARQRAEAAVLSGPGPPLGRAAQHGIPRPLSSAGRLSQGCRGASTVGAAGWKGELPKAGGSPAPGPETPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN |
| 预测分子量 | 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DUT重组蛋白的3篇参考文献示例(内容为模拟虚构，仅供参考)：
---
1. **文献名称**: *"High-yield expression and purification of recombinant DUT protein for structural studies"*
**作者**: Chen, L., et al.
**摘要**: 本研究报道了一种高效表达和纯化重组DUT蛋白的方法，通过大肠杆菌表达系统优化了可溶性表达条件，并利用亲和层析技术获得高纯度蛋白。通过X射线晶体学解析了DUT蛋白的三维结构，揭示了其催化活性位点的关键氨基酸残基，为后续酶学机制研究奠定了基础。
---
2. **文献名称**: *"Functional characterization of recombinant DUT in DNA repair pathways"*
**作者**: Smith, J., & Wang, H.
**摘要**: 文章通过体外实验验证了重组DUT蛋白在DNA损伤修复中的功能，发现其通过水解dUTP维持dTTP/dUTP的平衡，从而减少尿嘧啶在基因组中的错误掺入。研究还表明，DUT活性缺失会导致DNA断裂增加，提示其在基因组稳定性中的重要作用。
---
3. **文献名称**: *"Development of a DUT-deficient mouse model using recombinant protein-based gene editing"*
**作者**: Kimura, T., et al.
**摘要**: 利用CRISPR-Cas9技术结合重组DUT蛋白的体外功能验证，构建了DUT基因敲除小鼠模型。实验发现，DUT缺陷小鼠表现出胚胎致死表型，进一步分析揭示了DUT在早期胚胎发育中调控核苷酸代谢的关键作用，为相关疾病的机制研究提供了模型支持。
---
如需真实文献，建议通过PubMed或Web of Science搜索关键词 **"recombinant DUT protein"** 或 **"dUTPase expression"** 获取。
**Background of DUT Recombinant Protein**
DUT (deoxyuridine triphosphatase), also known as dUTP pyrophosphatase, is a critical enzyme involved in nucleotide metabolism and DNA replication. It catalyzes the hydrolysis of dUTP into dUMP and inorganic pyrophosphate, preventing the misincorporation of uracil into DNA during replication or repair. This function is essential for maintaining genomic stability, as excessive uracil in DNA can lead to mutagenesis or strand breaks.
The recombinant form of DUT is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to enable large-scale purification and functional studies. Recombinant DUT proteins retain enzymatic activity and are widely used to investigate DNA repair mechanisms, nucleotide pool regulation, and their roles in diseases like cancer. For instance, altered DUT expression has been linked to tumor progression, as cancer cells often exhibit dysregulated nucleotide metabolism to support rapid proliferation.
In research, DUT recombinant proteins serve as tools for structural studies, inhibitor screening, and understanding enzyme kinetics. Structural analyses using X-ray crystallography or cryo-EM have revealed conserved catalytic domains and mechanisms across species, aiding drug design. Additionally, DUT inhibitors are explored for their potential in chemotherapy, aiming to disrupt cancer cell DNA synthesis selectively.
Beyond oncology, DUT is studied in virology, as some viruses encode homologs to manipulate host nucleotide pools for replication. Recombinant DUT also aids in diagnostics, detecting autoantibodies in autoimmune disorders where DUT is a target antigen.
Overall, DUT recombinant protein bridges fundamental biology and translational applications, offering insights into genome integrity and therapeutic development. Its production and characterization remain pivotal for advancing studies in molecular biology and precision medicine.
×
