| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | INa |
| Uniprot No | Q16352 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-499aa |
| 氨基酸序列 | MSFGSEHYLCSSSSYRKVFGDGSRLSARLSGAGGAGGFRSQSLSRSNVASSAACSSASSLGLGLAYRRPPASDGLDLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRDLRAQLEEASSARSQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAEVDVTVAKPDLTSALREIRAQYESLAAKNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEERHSAEVAGYQDSIGQLENDLRNTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSTSGLSISGLNPLPNPSYLLPPRILSATTSKVSSTGLSLKKEEEEEEASKVASKKTSQIGESFEEILEETVISTKKTEKSNIEETTISSQKI |
| 预测分子量 | 55,3 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INa(钠离子通道)重组蛋白研究的3篇示例文献摘要，供参考：
1. **《Functional expression of recombinant voltage-gated sodium channels in mammalian cells》**
- 作者：Smith, J., et al.
- 摘要：研究通过将大鼠Nav1.2钠通道基因转染至HEK293细胞中实现重组表达，利用膜片钳技术分析通道的电生理特性，证实重组蛋白具有与天然通道相似的电压依赖性和快速失活特征。
2. **《High-yield production of human cardiac sodium channels in Drosophila S2 cells》**
- 作者：Lee, H., & Zhang, Y.
- 摘要：开发基于果蝇S2昆虫细胞系统的重组钠通道(hNav1.5)表达方法，通过优化培养条件显著提高蛋白产量，并验证其适用于药物靶点筛选及通道病机制研究。
3. **《Cryo-EM structure of the human Nav1.7 sodium channel bound to a toxin modulator》**
- 作者：Wang, R., et al.
- 摘要：利用冷冻电镜技术解析人源重组Nav1.7钠通道与蜘蛛毒素复合物的三维结构，揭示毒素结合位点及调控通道门控的分子机制，为镇痛药物设计提供结构基础。
注：以上文献为示例性概括，实际引用时需核实真实文献来源及内容准确性。
**Background of Recombinant INa Proteins**
Recombinant INa proteins, primarily referring to engineered voltage-gated sodium (Nav) channels, are critical tools for studying electrical signaling in excitable cells. Nav channels are transmembrane proteins responsible for initiating and propagating action potentials in neurons, muscles, and cardiac tissues. Their dysfunction is linked to disorders such as epilepsy, arrhythmias, and neuropathic pain.
Traditional studies relied on native channels isolated from tissues, but limitations in purity, quantity, and specificity drove the development of recombinant Nav proteins. Using heterologous expression systems (e.g., HEK293 or Xenopus oocytes), genes encoding specific Nav subtypes (e.g., Nav1.1–Nav1.9) are cloned and expressed. This allows precise control over subunit composition, post-translational modifications, and environmental conditions.
Recombinant INa proteins enable structure-function studies, including mapping pore domains, voltage sensors, and drug-binding sites. Techniques like cryo-EM and mutagenesis have revealed mechanisms of channel gating, inactivation, and toxin interactions. They also facilitate drug discovery by screening compounds for Nav subtype selectivity, critical for treating channelopathies without off-target effects.
Challenges remain, such as replicating native lipid environments and auxiliary subunit interactions. Nonetheless, recombinant INa systems are indispensable for deciphering Nav roles in physiology and disease, offering pathways to targeted therapies and personalized medicine. Advances in gene editing and computational modeling continue to enhance their utility in biomedical research.
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