| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SIRT2 |
| Uniprot No | Q8IXJ6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 50-356aa |
| 氨基酸序列 | MASSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDF RSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPT ICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCV SASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSC MQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPF LGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVR REHASIDAQSLEHHHHHH |
| 预测分子量 | 36 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SIRT2重组蛋白的3篇代表性文献(示例为模拟合成内容，仅供参考格式)：
1. **《Structural Insights into SIRT2 Substrate Specificity through Crystallographic Analysis》**
- **作者**: Smith A, et al.
- **摘要**: 通过重组表达人源SIRT2蛋白并解析其晶体结构，揭示了其底物结合口袋的关键氨基酸残基，阐明了其对特定乙酰化肽段的催化偏好性。
2. **《Development of a High-Yield Escherichia coli Expression System for Recombinant SIRT2 Production》**
- **作者**: Zhang L, et al.
- **摘要**: 报道了一种优化的原核表达体系，通过密码子优化和纯化策略改进，实现了SIRT2重组蛋白的高效可溶性表达，并验证了其体外去乙酰化酶活性。
3. **《SIRT2 Recombinant Protein Attenuates α-Synuclein Toxicity in Parkinson’s Disease Models》**
- **作者**: Johnson R, et al.
- **摘要**: 利用重组SIRT2蛋白处理帕金森病细胞模型，发现其通过去乙酰化α-突触核蛋白减少聚集，缓解神经元损伤，提示其治疗神经退行性疾病的潜力。
如需真实文献，建议通过PubMed或Google Scholar搜索关键词“SIRT2 recombinant protein”获取最新研究。
SIRT2. a member of the sirtuin family of NAD⁺-dependent deacetylases, plays multifaceted roles in cellular regulation and disease pathogenesis. Initially identified for its homology to yeast Sir2. SIRT2 primarily localizes to the cytoplasm but shuttles to the nucleus during specific phases of the cell cycle. It catalyzes the removal of acetyl groups from lysine residues on diverse substrates, including histones (e.g., H3K18. H4K16), α-tubulin, and metabolic enzymes like PARP3 and PKM2. linking it to chromatin remodeling, microtubule dynamics, and energy metabolism. SIRT2 is implicated in mitotic regulation, oxidative stress response, and aging, though its biological effects appear context-dependent. For instance, it may act as an oncogene by stabilizing c-Myc in certain cancers, yet exhibit tumor-suppressive properties in others by deacetylating p53.
Recombinant SIRT2 protein, typically produced in Escherichia coli or mammalian expression systems with affinity tags (e.g., His-tag), retains enzymatic activity for in vitro studies. Its production enables biochemical characterization of substrate specificity, kinetic parameters, and inhibitor screening—critical for drug development targeting age-related diseases. Structural studies using recombinant SIRT2 have revealed its catalytic domain architecture and mechanisms of allosteric regulation by NAD⁺ or synthetic modulators. Notably, SIRT2 inhibitors are being explored for neurodegenerative disorders (e.g., Parkinson’s disease) due to its role in α-synuclein aggregation, while activators may combat insulin resistance in metabolic syndromes. However, challenges persist in understanding tissue-specific effects and reconciling conflicting roles in diseases. Recombinant SIRT2 tools remain vital for resolving these complexities and advancing therapeutic strategies.
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