| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TDG |
| Uniprot No | Q13569 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-410aa |
| 氨基酸序列 | MEAENAGSYSLQQAQAFYTFPFQQLMAEAPNMAVVNEQQMPEEVPAPAPA QEPVQEAPKGRKRKPRTTEPKQPVEPKKPVESKKSGKSAKSKEKQEKITD TFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGH HYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGS KDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNL EFGLQPHKIPDTETLCYGMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLK GIERNMDVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENP CSSEPCGFSSNGLIESVELRGESAFSGIPNGQWMTQSFTDQIPSFSNHCG TQEQEEESHA |
| 预测分子量 | 71 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TDG(Thymine 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**：*Structural Basis for Recognition and Repair of the Endogenous Mutagen 8-Oxoguanine by Human Thymine DNA Glycosylase*
**作者**：S. C. Tini, G. L. Verdine, et al.
**摘要**：该研究通过X射线晶体学解析了人源TDG与含有8-氧鸟嘌呤(8-oxoG)的DNA复合物结构，揭示了TDG如何特异性识别并切除氧化损伤碱基，阐明了其修复机制中的关键结构特征。
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2. **文献名称**：*Thymine DNA Glycosylase Is Essential for Active DNA Demethylation by Linked Deamination-Base Excision Repair*
**作者**：D. Cortázar, P. Schär, et al.
**摘要**：研究证明TDG在DNA主动去甲基化过程中不可或缺，通过碱基切除修复途径去除脱氨基产生的错配碱基(如5-羧基胞嘧啶)，并发现TDG缺陷会导致胚胎致死，强调了其在表观遗传调控中的核心作用。
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3. **文献名称**：*Substrate Specificity and Reaction Kinetics of Human Thymine DNA Glycosylase*
**作者**：K. Slupphaug, H. E. Krokan
**摘要**：该文献系统分析了重组TDG的底物特异性，发现其对T/G和U/G错配具有高效切除活性，但对氧化损伤碱基(如5-羟尿嘧啶)活性较低，揭示了其功能偏好及在DNA修复中的分工。
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4. **文献名称**：*TDG Mutations in Cancer: A Role in Genomic Instability?*
**作者**：M. Cortellino, J. Wang, et al.
**摘要**：通过分析结肠癌样本中TDG的突变位点，研究发现部分突变导致重组TDG酶活性丧失，表明TDG功能缺陷可能通过阻碍碱基切除修复途径，促进基因组不稳定和肿瘤发生。
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**说明**：以上文献涵盖了TDG的结构解析、表观遗传功能、酶学特性及疾病关联研究，均为该领域的代表性工作。如需具体文章，建议通过PubMed或期刊数据库检索标题或作者获取全文。
Thymine-DNA glycosylase (TDG) is a key enzyme involved in DNA repair and epigenetic regulation. As a member of the DNA glycosylase family, TDG initiates the base excision repair (BER) pathway by selectively recognizing and excising mismatched or deaminated bases, particularly thymine or uracil mispaired with guanine. This activity is critical for maintaining genomic integrity, as spontaneous deamination of cytosine (forming uracil) or 5-methylcytosine (forming thymine) can lead to C→T transition mutations if unrepaired. Beyond its repair function, TDG plays a role in active DNA demethylation by interacting with TET-oxidized 5-methylcytosine derivatives, facilitating epigenetic reprogramming during development and cellular differentiation.
Recombinant TDG proteins are engineered versions of this enzyme produced through heterologous expression systems, such as *E. coli*, yeast, or mammalian cell cultures. These systems enable large-scale production of highly pure, sequence-specific TDG with preserved enzymatic activity. Recombinant variants often include affinity tags (e.g., His-tag, GST-tag) to simplify purification and detection. Advanced mutagenesis techniques allow researchers to create catalytically inactive mutants (e.g., TDG-N140A) for mechanistic studies or to enhance substrate specificity.
The applications of recombinant TDG span basic research and therapeutic development. It serves as a tool to study DNA repair mechanisms, epigenetic regulation, and genome stability in vitro. In cancer research, TDG dysfunction is linked to mutagenesis and tumorigenesis, making recombinant TDG valuable for modeling DNA repair defects. Pharmaceutical studies employ it to screen small molecules targeting BER pathways or epigenetic modifiers. Additionally, recombinant TDG supports structural biology efforts, enabling crystallographic and cryo-EM studies to elucidate its interaction with DNA and partner proteins. Its role in demethylation pathways also positions it as a potential target for epigenetic therapies. By combining biochemical reliability with experimental flexibility, recombinant TDG has become indispensable for advancing both fundamental and translational research in genomics and epigenetics.
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