| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | scn |
| Uniprot No | A7X482 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-116aa |
| 氨基酸序列 | STSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYKRTIKISGQKAMYALKSKDFKKMSEAKYQLQKIYNEIDEALKSKY |
| 预测分子量 | 17.2 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SCN重组蛋白的3篇代表性文献的简要概述：
1. **《Functional expression of recombinant human sodium channel SCN5A in HEK293 cells》**
- 作者：Smith J, et al.
- 摘要：本研究成功在HEK293细胞中表达了人源SCN5A重组钠通道蛋白，并通过膜片钳技术验证了其电生理活性，为心律失常相关药物筛选提供了可靠模型。
2. **《Cryo-EM structure of the human SCN1A channel reveals pathogenic mutation mechanisms》**
- 作者：Li X, et al.
- 摘要：利用冷冻电镜解析了SCN1A重组蛋白的高分辨率结构，揭示了癫痫相关突变如何破坏钠通道门控功能，为靶向治疗提供结构基础。
3. **《High-throughput screening of antiepileptic drugs using recombinant SCN2A variants》**
- 作者：Wang Y, et al.
- 摘要：通过表达携带不同突变的SCN2A重组蛋白，建立了高通量药物筛选平台，鉴定出可调节通道异常活性的潜在抗癫痫化合物。
(注：以上文献信息为示例，实际引用需根据具体研究补充准确信息。建议通过PubMed或Web of Science以关键词“SCN recombinant protein”或“voltage-gated sodium channel recombinant”检索最新文献。)
**Background of SCN Recombinant Proteins**
Recombinant SCN proteins are engineered versions of sodium channel proteins derived from the SCN gene family, which encode voltage-gated sodium channels (Nav) critical for electrical signaling in excitable cells. These channels regulate sodium ion flow across cell membranes, enabling action potentials in neurons, muscles, and cardiac tissues. Dysfunctional SCN proteins are linked to disorders such as epilepsy, arrhythmias, and chronic pain syndromes, making them key therapeutic targets.
The development of recombinant SCN proteins emerged alongside advances in genetic engineering and structural biology. Traditional studies relied on isolating native channels from tissues, but low abundance and heterogeneity limited progress. Recombinant technology, utilizing expression systems like *E. coli*, insect cells, or mammalian cell lines (e.g., HEK293), enabled large-scale production of purified, homogeneous SCN proteins. This breakthrough facilitated detailed studies of channel structure-function relationships, drug interactions, and disease mechanisms.
Key milestones include the cloning of SCN genes in the 1980s-1990s and the subsequent use of recombinant proteins to map binding sites for toxins (e.g., tetrodotoxin) and anticonvulsant drugs. Cryo-EM and X-ray crystallography later revealed atomic-level details of Nav channels, with recombinant SCN proteins serving as essential tools. Today, these proteins underpin drug discovery for pain management and channelopathies, while engineered mutants help dissect pathogenic variants. Challenges remain in preserving post-translational modifications and functional stability *in vitro*, driving ongoing innovation in expression and purification strategies. Recombinant SCN proteins thus represent a cornerstone of neuroscience and pharmacology research.
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