| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | nth |
| 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 | MCSPQESGMT ALSARMLTRS RSLGPGAGPR GCREEPGPLR RREAAAEARK SHSPVKRPRK AQRLRVAYEG SDSEKGEGAE PLKVPVWEPQ DWQQQLVNIR AMRNKKDAPV DHLGTEHCYD SSAPPKVRRY QVLLSLMLSS QTKDQVTAGA MQRLRARGLT VDSILQTDDA TLGKLIYPVG FWRSKVKYIK QTSAILQQHY GGDIPASVAE LVALPGVGPK MAHLAMAVAW GTVSGIAVDT HVHRIANRLR WTKKATKSPE ETRAALEEWL PRELWHEING LLVGFGQQTC LPVHPRCHAC LNQALCPAAQ GL |
| 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Nth(Endonuclease III)重组蛋白的3篇参考文献示例(内容为虚构，仅作格式参考)：
1. **文献名称**：*Cloning and Expression of Escherichia coli Nth Gene in a Recombinant System*
**作者**：H. Ide, T. Yamamoto
**摘要**：该研究报道了利用大肠杆菌表达系统克隆并纯化Nth重组蛋白，验证了其特异性识别和切除氧化损伤DNA碱基(如胸腺嘧啶乙二醇)的活性，为后续酶学分析奠定基础。
2. **文献名称**：*Crystal Structure of Recombinant Nth Protein Reveals Substrate Binding Mechanism*
**作者**：A.K. McCullough, M.L. Dodson
**摘要**：通过X射线晶体学解析了重组Nth蛋白的三维结构，揭示了其保守的螺旋-发夹-螺旋结构域在DNA损伤识别中的作用，阐明了催化位点关键氨基酸的功能。
3. **文献名称**：*Functional Analysis of Recombinant Nth in Oxidative Stress Repair Pathways*
**作者**：M. Dizdaroglu, J.H. Bielski
**摘要**：利用重组Nth蛋白探究了其在体外修复8-氧代鸟嘌呤等氧化损伤的动力学特性，发现其与人类同源酶OGG1的功能互补性，提示跨物种修复机制的保守性。
4. **文献名称**：*Application of Recombinant Nth in Gene Therapy for DNA Damage Repair*
**作者**：S. David, R.P. Cunningham
**摘要**：评估了重组Nth蛋白在哺乳动物细胞中增强基因组稳定性的潜力，证明其递送可减少氧化应激诱导的突变，为基因编辑工具开发提供新思路。
(注：以上文献为示例性内容，实际引用时请核实真实论文信息。)
Nth (endonuclease III-like protein 1) is a DNA repair enzyme belonging to the helix-hairpin-helix (HhH) superfamily, primarily involved in base excision repair (BER) pathways. It was first identified in *E. coli* as a key player in repairing oxidative DNA damage, and homologs have since been found across eukaryotes, including humans. The enzyme specifically targets and removes oxidized pyrimidines, such as thymine glycol, 5-hydroxycytosine, and dihydrouracil, which are common lesions caused by reactive oxygen species (ROS) or ionizing radiation. Its bifunctional activity combines glycosylase action (cleaving the N-glycosidic bond of damaged bases) and β-lyase activity (nicking the DNA backbone), creating a single-strand break to initiate repair.
Recombinant Nth proteins are produced using expression systems like *E. coli* or yeast, enabling large-scale purification for structural and functional studies. Crystallographic analyses have revealed its conserved structural motifs, including the HhH domain for DNA binding and an iron-sulfur cluster critical for redox sensing. Research on recombinant Nth has advanced our understanding of oxidative DNA damage tolerance mechanisms and their links to aging, cancer, and neurodegenerative diseases. For example, mutations in human homologs (e.g., NTHL1) are associated with inherited colorectal cancer syndromes, highlighting its role in genome stability.
In biotechnology, engineered Nth variants are explored for applications in DNA diagnostics and synthetic biology tools. Studies also investigate its interaction with other BER proteins (e.g., APE1. Pol β) to map repair pathway crosstalk. The development of Nth inhibitors is being pursued to sensitize cancer cells to radiotherapy. Overall, recombinant Nth serves as a vital model for dissecting DNA repair mechanisms and developing therapeutic strategies against oxidative stress-related disorders.
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