| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NKA |
| Uniprot No | P20366 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-129aa |
| 氨基酸序列 | MKILVALAVFFLVSTQLFAEEIGANDDLNYWSDWYDSDQIKEELPEPFEHLLQRIARRPKPQQFFGLMGKRDADSSIEKQVALLKALYGHGQISHKRHKTDSFVGLMGKRALNSVAYERSAMQNYERRR |
| 预测分子量 | 42.0 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NKA(Na⁺/K⁺-ATP酶)重组蛋白研究的3篇参考文献示例(信息为模拟概括，非真实文献)：
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1. **文献名称**：*Expression and functional characterization of recombinant Na⁺/K⁺-ATPase in mammalian cells*
**作者**：Shinoda T. et al.
**摘要**：研究通过哺乳动物细胞系统重组表达了NKA蛋白，解析了其α和β亚基的共表达机制，并验证了重组蛋白的离子转运活性和对强心苷类药物的敏感性。
2. **文献名称**：*Role of the β-subunit in the stability of Na⁺/K⁺-ATPase: Insights from recombinant chimeric proteins*
**作者**：Geering K., Lingrel J.B.
**摘要**：通过构建嵌合体重组蛋白，揭示了β亚基对NKA结构稳定性及膜定位的关键作用，并探讨不同亚型(如α1、α2)的功能差异。
3. **文献名称**：*Recombinant Na⁺/K⁺-ATPase isoforms: Comparative analysis of enzymatic kinetics and ATP hydrolysis*
**作者**：Crambert G., Cornelius F.
**摘要**：比较了重组表达的NKA不同亚型(α1/β1 vs. α3/β2)的酶动力学特性，发现α3亚型在高钠环境下的ATP水解效率显著提升，提示其组织特异性功能。
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如需真实文献，建议通过PubMed或Google Scholar搜索关键词如 **"recombinant Na+/K+-ATPase"** 或 **"NKA expression and purification"**。
**Background of NKA Recombinant Proteins**
Na+/K+-ATPase (NKA), a critical transmembrane enzyme, plays a central role in maintaining cellular ion homeostasis by actively transporting Na+ out and K+ into cells using ATP hydrolysis. This electrochemical gradient is essential for numerous physiological processes, including nerve impulse transmission, muscle contraction, and secondary solute transport. Structurally, NKA consists of α, β, and γ subunits, with the α-subunit harboring catalytic activity and the β-subunit ensuring proper membrane integration. Dysregulation of NKA is linked to pathologies such as heart failure, neurological disorders, and kidney diseases.
Recombinant NKA proteins are engineered to study its structure-function relationships, regulatory mechanisms, and interactions with drugs or endogenous modulators. Traditional purification of NKA from native tissues faces challenges like low yield and contamination. Recombinant technology, using expression systems (e.g., mammalian cells, yeast, or insect cells), enables scalable production of high-purity, functional NKA variants. Tagging strategies (e.g., His-tags) facilitate purification and tracking.
Research applications include elucidating NKA’s role in diseases, screening cardiotonic steroids (e.g., ouabain) as potential therapeutics, and exploring its signaling functions beyond ion transport. Recent advances in cryo-EM and X-ray crystallography using recombinant NKA have resolved atomic-level structures, revealing mechanisms of ion transport and drug binding. Challenges persist in mimicking native lipid environments and post-translational modifications *in vitro*, necessitating optimized expression systems.
Overall, recombinant NKA proteins are indispensable tools for bridging molecular insights with therapeutic innovation, offering a platform to dissect its biological significance and exploit its clinical potential.
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