| 纯度 | >90%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | ung |
| Uniprot No | P12295 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-229aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMANELTW HDVLAEEKQQ PYFLNTLQTV ASERQSGVTI YPPQKDVFNA FRFTELGDVK VVILGQDPYH GPGQAHGLAF SVRPGIAIPP SLLNMYKELE NTIPGFTRPN HGYLESWARQ GVLLLNTVLT VRAGQAHSHA SLGWETFTDK VISLINQHRE GVVFLLWGSH AQKKGAIIDK QRHHVLKAPH PSPLSAHRGF FGCNHFVLAN QWLEQRGETP IDWMPVLPAE SE |
| 预测分子量 | 28 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UNG(尿嘧啶-DNA糖基化酶)重组蛋白的3篇代表性文献(示例格式，非真实文献)：
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1. **文献名称**：*Production and characterization of recombinant human uracil-DNA glycosylase*
**作者**：Smith J, et al.
**摘要**：本研究描述了大肠杆菌表达系统中重组人UNG蛋白的高效表达与纯化方法，验证了其特异性切割DNA中尿嘧啶残基的活性，并证明其在PCR污染控制中的应用潜力。
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2. **文献名称**：*Structural insights into the substrate recognition mechanism of UNG enzyme*
**作者**：Chen L, Wang H.
**摘要**：通过X射线晶体学解析了重组UNG蛋白与含尿嘧啶DNA复合物的结构，揭示了其底物识别和催化机制，为设计基于UNG的基因编辑工具提供理论依据。
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3. **文献名称**：*UNG-deficient mice model generated by recombinant protein-based gene targeting*
**作者**：Tanaka K, et al.
**摘要**：利用重组UNG蛋白验证基因敲除小鼠模型的DNA修复缺陷表型，证实UNG在维持基因组稳定性中的关键作用及其与癌症发生的关系。
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(注：以上内容为模拟示例，实际文献需通过PubMed/Google Scholar检索关键词"recombinant uracil-DNA glycosylase"或"UNG protein expression"获取。)
**Background of UNG Recombinant Protein**
Uracil-DNA glycosylase (UNG) is a highly conserved enzyme critical in DNA repair, specifically excising uracil residues that arise in DNA through spontaneous deamination of cytosine or misincorporation of dUTP during replication. Its role in maintaining genomic integrity makes it essential for preventing C→T mutagenesis and ensuring accurate DNA replication.
Recombinant UNG proteins are engineered versions of the enzyme produced via heterologous expression systems, such as *E. coli* or eukaryotic cells, enabling large-scale purification for research and therapeutic applications. The human UNG gene encodes two major isoforms: UNG1 (mitochondrial) and UNG2 (nuclear), differing in subcellular localization and function. Recombinant UNG retains the enzymatic activity of its native counterpart, specifically cleaving the glycosidic bond of uracil in single- or double-stranded DNA without damaging the phosphodiester backbone.
In molecular biology, recombinant UNG is widely used in PCR-based techniques (e.g., cloning, qPCR) to prevent carryover contamination by degrading uracil-containing templates from previous reactions. It also serves as a tool to study DNA repair mechanisms, genome stability, and mutagenesis. In therapeutics, UNG has been explored as a target for cancer treatment, as cancer cells with defective repair pathways may rely on UNG activity for survival. Additionally, its role in viral DNA processing (e.g., HIV, herpesviruses) positions it as a potential antiviral target.
Quality-controlled recombinant UNG is characterized for purity, activity, and stability, ensuring reproducibility in experiments. Its specificity and efficiency under diverse conditions (e.g., temperature, buffer compatibility) make it indispensable in both basic research and biotechnological applications.
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