| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | AURKA |
| Uniprot No | O14965 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-403aa |
| 氨基酸序列 | MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS |
| 预测分子量 | 51.8 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3篇关于AURKA重组蛋白的参考文献及其摘要概括：
1. **"Structural Basis of Aurora-A Activation by TPX2 at the Mitotic Spindle"**
- Bayliss, R., et al. (2003).
- 该研究解析了重组AURKA蛋白与激活因子TPX2的复合物晶体结构，揭示了TPX2诱导AURKA构象变化和自磷酸化的分子机制，为阐明其在有丝分裂中的功能提供结构基础。
2. **"Expression, Purification, and Biochemical Characterization of Human Aurora Kinase A"**
- Walter, A.O., et al. (2000).
- 报道了人源AURKA重组蛋白在大肠杆菌中的表达与纯化方法，并系统分析了其激酶活性及ATP结合特性，为后续药物筛选研究提供了可靠的重组蛋白工具。
3. **"Aurora-A Kinase Inhibitor Screening Using a Reconstituted Protein Phosphorylation Cascade"**
- Fu, J., et al. (2009).
- 开发了一种基于重组AURKA蛋白的体外磷酸化级联反应系统，用于高通量筛选激酶抑制剂，验证了多个候选化合物对AURKA活性的抑制作用及其抗癌潜力。
如需具体文献链接或更多信息，可补充数据库名称(如PubMed ID)进一步查询。
Aurora kinase A (AURKA), a member of the serine/threonine kinase family, plays a critical role in regulating mitotic progression, including centrosome maturation, spindle assembly, and chromosomal segregation. Overexpression or dysregulation of AURKA is strongly associated with tumorigenesis, metastasis, and therapeutic resistance in various cancers, making it a promising therapeutic target. To study its biochemical functions and develop targeted therapies, recombinant AURKA protein is widely utilized in research.
Recombinant AURKA is typically produced using heterologous expression systems, such as *E. coli* or mammalian cell lines, to ensure high purity and functional activity. The protein often includes affinity tags (e.g., GST, His-tag) for simplified purification and detection. Its kinase activity is frequently validated through phosphorylation assays using substrates like histone H3 or TPX2. Researchers employ recombinant AURKA to investigate enzymatic kinetics, screen small-molecule inhibitors, and explore protein-protein interactions.
In drug discovery, recombinant AURKA serves as a tool to evaluate inhibitor efficacy and selectivity, aiding the development of anticancer agents. Structural studies using recombinant protein have also elucidated mechanisms of kinase activation and resistance mutations. Challenges in working with AURKA include maintaining its labile conformation and post-translational modifications (e.g., auto-phosphorylation), which may require optimized expression systems or co-expression with stabilizing partners.
Overall, recombinant AURKA remains indispensable for both basic research and translational applications, bridging mechanistic insights into mitotic regulation and clinical advancements in oncology.
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