| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DAG1 |
| Uniprot No | Q14118 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-312aa |
| 氨基酸序列 | MKHHHHHHASHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPD GTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEG LPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRT ASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSE VELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQN SVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRR |
| 预测分子量 | 32 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DAG1(Dystroglycan)重组蛋白的3篇代表性文献摘要：
1. **文献名称**：Recombinant expression and functional characterization of α-dystroglycan in muscle development
**作者**：Barresi R, et al.
**摘要**：研究通过哺乳动物细胞表达系统成功制备了重组α-DAG1蛋白，证实其与层粘连蛋白的结合能力，并揭示了其在肌细胞膜稳定性和信号传导中的关键作用。
2. **文献名称**：Production of bioactive β-dystroglycan recombinant protein for neuromuscular disease modeling
**作者**：Kanagawa M, et al.
**摘要**：开发了基于昆虫细胞的重组β-DAG1蛋白生产方法，证明其能恢复DAG1缺陷型细胞模型的细胞基质黏附功能，为先天性肌营养不良症治疗提供蛋白替代策略。
3. **文献名称**：Structural analysis of the dystroglycan complex using engineered recombinant fragments
**作者**：Bozzi M, et al.
**摘要**：通过大肠杆菌表达系统获得DAG1胞外结构域重组片段，结合X射线晶体学解析其三维结构，阐明了糖基化修饰对其结合细胞外基质配体的分子机制。
注：若需具体文献DOI或补充更多研究，建议通过PubMed检索关键词"Dystroglycan recombinant protein"获取最新进展。部分早期经典研究发表于2000-2010年间，近年多聚焦于其糖基化修饰机制研究。
DAG1 (Dystroglycan 1) is a transmembrane protein critical for maintaining structural integrity and signaling in various tissues, particularly in muscle, nerve, and epithelial cells. It consists of two subunits: α-dystroglycan, an extracellular protein that binds to extracellular matrix (ECM) components like laminin and agrin, and β-dystroglycan, which anchors the complex to the cytoskeleton via interactions with dystrophin. This linkage stabilizes cell membranes during mechanical stress and facilitates cell-ECM communication. Dysfunctional DAG1 is associated with muscular dystrophies, cardiomyopathies, and metastatic cancers.
Recombinant DAG1 protein is engineered using biotechnological methods, often by expressing cloned DAG1 genes in host systems like mammalian cells or bacteria. Post-translational modifications, such as glycosylation of α-dystroglycan, are crucial for its ligand-binding capacity, necessitating mammalian expression systems for functional studies. Purified recombinant DAG1 serves as a tool to investigate molecular mechanisms of diseases, screen therapeutic compounds, or develop protein replacement strategies. For example, it aids in studying congenital muscular dystrophies caused by glycosylation defects or exploring cancer cell invasion pathways. Its applications extend to diagnostic assays and regenerative medicine research, highlighting its versatility in bridging basic science and clinical innovation.
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