| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AEN |
| Uniprot No | Q8WTP8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 117-325aa |
| 氨基酸序列 | MVGTGPRGRVSELARCSIVSYHGNVLYDKYIRPEMPIADYRTRWSGITRQHMRKAVPFQVAQKEILKLLKGKVVVGHALHNDFQALKYVHPRSQTRDTTYVPNFLSEPGLHTRARVSLKDLALQLLHKKIQVGQHGHSSVEDATTAMELYRLVEVQWEQQEARSLWTCPEDREPDSSTDMEQYMEDQYWPDDLAHGSRGGAREAQDRRN |
| 预测分子量 | 40.1kDa |
| 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. |
以下为3篇关于AEN重组蛋白的参考文献示例(文献信息为虚拟合成，仅供格式参考)：
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1. **文献名称**: *"Recombinant AEN Protein Induces DNA Fragmentation in Apoptotic Cells"*
**作者**: Zhang L. et al.
**摘要**: 研究团队通过大肠杆菌表达系统成功纯化AEN重组蛋白，证实其具有核酸内切酶活性，可诱导肿瘤细胞DNA断裂并促进凋亡，为癌症治疗提供潜在靶点。
2. **文献名称**: *"Structural Characterization and Functional Analysis of AEN in p53-Dependent Apoptosis"*
**作者**: Tanaka K. et al.
**摘要**: 通过X射线晶体学解析AEN重组蛋白的3D结构，揭示其与p53蛋白的相互作用机制，阐明AEN在DNA损伤应答中增强细胞凋亡的分子通路。
3. **文献名称**: *"AEN Recombinant Protein Enhances Chemosensitivity in Glioblastoma Models"*
**作者**: Wang Y. & Chen R.
**摘要**: 在胶质母细胞瘤小鼠模型中，局部注射AEN重组蛋白显著增强顺铂的化疗效果，证实其通过抑制DNA修复通路提高肿瘤细胞对基因毒药物的敏感性。
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注：以上文献为示例，实际研究中请通过PubMed、Web of Science等数据库检索真实发表的论文。
AEN recombinant protein, derived from the Apoptosis-Enhancing Nuclease (AEN) gene, is a genetically engineered protein with critical roles in DNA damage response and apoptosis regulation. AEN, also known as DFFB-like endonuclease 1 (DFFB), is a member of the DNA fragmentation factor (DFF) family. It functions as a nuclease that promotes apoptotic DNA fragmentation and chromatin condensation, processes essential for programmed cell death. The protein is activated during cellular stress, such as UV radiation or chemotherapeutic exposure, where it cleaves genomic DNA into characteristic fragments, a hallmark of apoptosis.
Researchers produce AEN recombinant protein using expression systems like E. coli or mammalian cells, enabling studies of its enzymatic activity and interactions with apoptotic regulators such as caspases and DFF45/ICAD. Its recombinant form retains endonuclease activity, making it valuable for in vitro assays investigating DNA repair mechanisms, cancer biology, and cytotoxic drug responses. Notably, AEN dysregulation has been implicated in cancer progression, neurodegenerative diseases, and resistance to chemotherapy, positioning it as a potential therapeutic target or biomarker.
Recent studies explore AEN's dual roles beyond apoptosis, including involvement in innate immunity and inflammatory responses. Its ability to process cytoplasmic DNA also links it to autoimmune disorders like lupus. However, challenges remain in fully elucidating its structure-function relationships and tissue-specific regulatory networks. Current applications span drug discovery, gene editing tools, and diagnostic development, underscoring its multifaceted significance in biomedical research.
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