| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MPG |
| Uniprot No | P29372 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-298aa |
| 氨基酸序列 | MVTPALQMKKPKQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSD AAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLAR AFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMF MKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTL RKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLE PSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQALE HHHHHH |
| 预测分子量 | 34 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3篇关于MPG(N-Methylpurine DNA Glycosylase)重组蛋白的参考文献及其摘要概括：
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1. **文献名称**：*"Production and characterization of recombinant human MPG protein for DNA repair studies"*
**作者**：Smith J, et al.
**摘要**：该研究报道了通过大肠杆菌表达系统高效表达和纯化重组人源MPG蛋白的方法，并验证其在体外特异性识别并切除DNA链中烷基化损伤碱基(如3-methyladenine)的活性，为DNA修复机制研究提供工具。
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2. **文献名称**：*"Structural insights into substrate specificity of MPG protein through crystallographic analysis"*
**作者**：Chen L, Wang H.
**摘要**：通过X射线晶体学解析了重组MPG蛋白与损伤DNA复合物的三维结构，揭示了其底物结合口袋的关键氨基酸残基如何选择性识别不同烷基化损伤，为设计靶向MPG的小分子抑制剂奠定基础。
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3. **文献名称**：*"MPG recombinant protein enhances gene targeting efficiency in CRISPR-mediated genome editing"*
**作者**：Kimura R, et al.
**摘要**：研究发现将重组MPG蛋白与CRISPR-Cas9系统联用，可通过局部增强DNA损伤修复机制，显著提高同源重组修复效率，为基因治疗和功能基因组学提供新策略。
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(注：以上文献为示例性内容，实际引用需以真实出版物为准。)
MPG (Methylpurine DNA Glycosylase), also known as N-methylpurine DNA glycosylase or ANPG, is a critical enzyme involved in DNA repair mechanisms. It belongs to the base excision repair (BER) pathway, which addresses small, non-helix-distorting DNA lesions caused by alkylation, oxidation, or deamination. Discovered in the 1990s, MPG specifically recognizes and excises damaged bases such as 3-methyladenine, 7-methylguanine, and hypoxanthine, initiating repair by cleaving the N-glycosidic bond between the damaged base and the sugar-phosphate backbone. This activity is essential for maintaining genomic stability and preventing mutagenesis.
The recombinant MPG protein, produced via genetic engineering in bacterial or eukaryotic expression systems, has become a valuable tool in molecular biology and therapeutic research. Recombinant technology allows large-scale production with high purity, enabling researchers to study its substrate specificity, enzymatic kinetics, and interactions with other BER components. Its applications extend to in vitro DNA repair assays, diagnostic kits for DNA damage detection, and potential use in gene therapy to enhance cellular repair capacity.
In cancer research, MPG’s role is dual-edged. While it protects cells from mutagenic damage, overexpression may interfere with chemotherapy agents that rely on DNA alkylation (e.g., temozolomide), prompting studies into MPG inhibitors as chemosensitizers. Conversely, recombinant MPG has been explored in gene-editing workflows to reduce DNA damage artifacts. Despite progress, challenges remain in optimizing its stability, delivery efficiency, and tissue-specific targeting for clinical applications. Ongoing research aims to harness MPG’s repair capabilities while balancing its biological complexity in therapeutic contexts.
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