| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AD |
| Uniprot No | P23793 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-410aa |
| 氨基酸序列 | SVFDSKFKGIHVYSEIGELESVLVHEPGREIDYITPARLDELLFSAILES HDARKEHKQFVAELKANDINVVELIDLVAETYDLASQEAKDKLIEEFLED SEPVLSEEHKVVVRNFLKAKKTSRELVEIMMAGITKTDLGIEADHELIVD PMPNLYFTRDPFASVGNGVTIHYMRYKVRQRETLFSRFVFSNHPKLINTP WYYDPSLKLSIEGGDVFIYNNDTLVVGVSERTDLQTVTLLAKNIVANKEC EFKRIVAINVPKWTNLMHLDTWLTMLDKDKFLYSPIANDVFKFWDYDLVN GGAEPQPVENGLPLEGLLQSIINKKPVLIPIAGEGASQMEIERETHFDGT NYLAIRPGVVIGYSRNEKTNAALEAAGIKVLPFHGNQLSLGMGNARCMSM PLSRKDVKW |
| 预测分子量 | 46 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. |
以下是关于阿尔茨海默病(AD)重组蛋白研究的3篇参考文献的简要总结(注：以下为模拟示例，非真实文献)：
1. **《重组β-淀粉样蛋白的表达及其在AD模型中的毒性研究》**
- 作者：Smith J, et al.
- 摘要：研究通过大肠杆菌系统表达重组Aβ42蛋白，分析其聚集特性，并证明其在体外神经元细胞中诱导氧化应激和突触毒性，为AD病理机制提供模型支持。
2. **《重组Tau蛋白磷酸化调控及其对神经纤维缠结形成的影响》**
- 作者：Zhang L, et al.
- 摘要：利用昆虫细胞系统表达重组人源Tau蛋白，探讨激酶介导的磷酸化修饰如何促进Tau异常聚集，揭示其在AD神经纤维缠结形成中的关键作用。
3. **《基于重组Aβ的单克隆抗体开发及其治疗AD的潜力》**
- 作者：Patel R, et al.
- 摘要：通过哺乳动物细胞表达重组Aβ单体，制备特异性单克隆抗体，并在转基因小鼠模型中验证其减少淀粉样斑块沉积和改善认知功能的效果。
4. **《重组蛋白片段在AD早期诊断中的应用》**
- 作者：Kim S, et al.
- 摘要：设计并表达AD相关重组蛋白片段(如Aβ1-16和Tau N端结构域)，开发高灵敏度ELISA检测方法，用于患者脑脊液和血液中生物标志物的定量分析。
(注：以上内容为示例性概括，实际文献需通过学术数据库查询。)
**Background of AD Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biomedical research and therapeutic development. Among these, AD (Activation Domain) recombinant proteins hold particular significance in studying protein-protein interactions and cellular signaling pathways. The AD, a functional protein domain often derived from transcription factors, is characterized by its ability to activate gene expression by recruiting transcriptional machinery. This domain is widely utilized in systems like the yeast two-hybrid (Y2H) assay, where it is fused to a protein of interest to detect interactions with other molecules. When interaction occurs, the AD triggers reporter gene expression, enabling researchers to map interactomes or validate suspected binding partners.
The development of AD recombinant proteins relies on advanced cloning techniques, such as PCR amplification, restriction enzyme-based assembly, or seamless cloning methods like Gibson Assembly. These proteins are typically expressed in heterologous systems (e.g., *E. coli*, mammalian cells) and purified via affinity tags (e.g., His-tag, GST-tag). Structural and functional studies of AD-containing proteins have deepened our understanding of transcriptional regulation, post-translational modifications, and disease mechanisms linked to dysregulated signaling.
Beyond basic research, AD recombinant proteins are pivotal in drug discovery. They serve as tools for high-throughput screening of compounds targeting specific interactions or pathways. For instance, AD-fused oncoproteins help identify inhibitors in cancer research. Additionally, engineered AD variants are explored in synthetic biology to design programmable transcription factors, enabling precise control of gene expression in gene therapy or metabolic engineering.
Despite challenges like solubility and stability, advancements in protein engineering, such as directed evolution or computational design, continue to enhance the utility of AD recombinant proteins. Their versatility underscores their role as indispensable tools in both academic and industrial settings, bridging molecular biology and translational applications.
×
