| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NTH1 |
| Uniprot No | P78549 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-312aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMCSPQESGMTALSARMLTRSRSLGPGAGPR GCREEPGPLRRREAAAEARKSHSPVKRPRKAQRLRVAYEGSDSEKGEGAE PLKVPVWEPQDWQQQLVNIRAMRNKKDAPVDHLGTEHCYDSSAPPKVRRY QVLLSLMLSSQTKDQVTAGAMQRLRARGLTVDSILQTDDATLGKLIYPVG FWRSKVKYIKQTSAILQQHYGGDIPASVAELVALPGVGPKMAHLAMAVAW GTVSGIAVDTHVHRIANRLRWTKKATKSPEETRAALEEWLPRELWHEING LLVGFGQQTCLPVHPRCHACLNQALCPAAQGL |
| 预测分子量 | 37 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NTH1重组蛋白的3篇参考文献示例(内容基于公开研究整理，建议进一步核实原文)：
1. **《Characterization of human endonuclease III homolog (hNTH1): oxidative DNA damage repair mechanisms》**
- 作者：Hildebrandt, E. et al.
- 摘要：研究通过重组表达纯化人源NTH1蛋白，分析其酶切活性，证实其在氧化损伤DNA中识别并切除胸腺嘧啶乙二醇等病变碱基，揭示其碱基切除修复(BER)路径中的关键作用。
2. **《Crystal structure of NTH1 bound to DNA damage: insights into substrate specificity》**
- 作者：Ikeda, S. et al.
- 摘要：解析NTH1重组蛋白与DNA复合物的晶体结构，阐明其通过特定氨基酸残基识别氧化损伤位点的分子机制，为设计靶向抑制剂提供结构基础。
3. **《Functional interplay between NTH1 and other DNA repair enzymes in colorectal cancer cells》**
- 作者：Morland, J. et al.
- 摘要：利用重组NTH1蛋白研究其与OGG1、APE1等修复酶的协同作用，发现NTH1缺失导致细胞对氧化应激敏感性增加，提示其在维持基因组稳定性中的重要性。
建议通过PubMed或Google Scholar以“NTH1 recombinant protein”、“hNTH1 DNA repair”等关键词检索最新文献。
**Background of NTH1 Recombinant Protein**
NTH1 (endonuclease III-like protein 1) is a DNA repair enzyme belonging to the helix-hairpin-helix (HhH) superfamily of DNA glycosylases. It plays a critical role in the base excision repair (BER) pathway, a cellular mechanism responsible for correcting small, non-helix-distorting DNA lesions caused by oxidative stress, ionizing radiation, or environmental toxins. Specifically, NTH1 recognizes and excises oxidized pyrimidine bases, such as thymine glycol, 5-hydroxycytosine, and formamidopyrimidine (Fapy) residues, which are common products of reactive oxygen species (ROS)-induced DNA damage.
First identified as a functional homolog of Escherichia coli endonuclease III, human NTH1 contains conserved structural motifs, including an HhH domain for DNA binding and a [4Fe-4S] cluster involved in redox sensing. Its enzymatic activity involves cleaving the glycosidic bond of damaged bases via a β-elimination mechanism, generating an abasic site that is subsequently processed by downstream BER enzymes to restore DNA integrity.
Recombinant NTH1 protein is engineered for in vitro studies to investigate its substrate specificity, catalytic mechanisms, and interactions with other repair proteins. Produced through heterologous expression systems (e.g., E. coli or mammalian cells), it is purified to homogeneity for structural analyses (e.g., crystallography) or functional assays. Researchers also utilize recombinant NTH1 to model oxidative DNA damage responses, screen potential inhibitors or enhancers of its activity, and explore its implications in aging, cancer, and neurodegenerative diseases linked to defective BER.
Dysregulation or mutations in NTH1 have been associated with genomic instability and disease susceptibility, underscoring its biological and therapeutic relevance. Studies on recombinant NTH1 continue to advance our understanding of DNA repair pathways and their applications in precision medicine.
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