| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FEN1 |
| Uniprot No | P39748 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-380aa |
| 氨基酸序列 | MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK |
| 预测分子量 | 50.0 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FEN1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：Functional analysis of human FEN1 in chromatin assembly and DNA replication
**作者**：Harrington, J. J., Lieber, M. R.
**摘要**：研究利用重组人FEN1蛋白，揭示了其在DNA复制过程中对“flap”结构的切割活性，并证明其与PCNA(增殖细胞核抗原)的相互作用对染色质组装至关重要。
2. **文献名称**：Structural basis of FEN1 nuclease activity in DNA replication and repair
**作者**：Sakurai, S., et al.
**摘要**：通过X射线晶体学解析了重组FEN1蛋白的三维结构，阐明了其底物识别和催化机制，为设计靶向FEN1的癌症治疗策略提供依据。
3. **文献名称**：Reconstitution of the FEN1/PCNA interaction and its role in long-patch base excision repair
**作者**：Klungland, A., Lindahl, T.
**摘要**：通过体外重组蛋白实验，验证了FEN1与PCNA的功能协同性，证明两者结合是碱基切除修复中长片段修复途径的必要条件。
(注：以上文献信息为示例，实际引用需核对原文准确性。)
**Background of FEN1 Recombinant Protein**
Flap endonuclease 1 (FEN1) is a structure-specific nuclease critical for maintaining genomic stability in eukaryotic cells. It plays a central role in DNA replication and repair, particularly in processing Okazaki fragments during lagging-strand synthesis and resolving 5' flap structures formed during long-patch base excision repair. FEN1 cleaves 5' overhangs or displaced DNA flaps with high precision, ensuring seamless ligation of DNA strands. Its dysfunction is linked to genomic instability, cancer predisposition, and neurodegenerative disorders.
The recombinant FEN1 protein is engineered using biotechnological methods to enable high-purity, scalable production for research and therapeutic applications. Typically, the *FEN1* gene is cloned into expression vectors (e.g., *E. coli* or insect cell systems) and purified via affinity chromatography. Recombinant FEN1 retains enzymatic activity, allowing in vitro studies of substrate specificity, interaction partners (e.g., PCNA, APE1), and mechanisms in DNA repair pathways.
Research applications include investigating FEN1's role in cancer biology, where overexpression correlates with tumor aggressiveness and chemoresistance, making it a potential therapeutic target. Inhibitors of FEN1 are being explored to sensitize cancer cells to DNA-damaging agents. Additionally, recombinant FEN1 is used in synthetic biology for designing DNA assembly tools and diagnostics, such as detecting nucleic acid mutations. Structural studies using recombinant protein have revealed its conserved catalytic core, helical clamp, and divalent metal ion (Mg²⁺/Zn²⁺) dependency, advancing understanding of nuclease evolution.
Overall, FEN1 recombinant protein serves as a vital tool for dissecting DNA metabolism mechanisms and developing biomedical interventions.
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