| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHRNa1 |
| Uniprot No | P02708 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-255aa |
| 氨基酸序列 | SEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIV TTNVRLKQGDMVDLPRPSCVTLGVPLFSHLQNEQWVDYNLKWNPDDYGGV KKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFK SYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGE WVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRL |
| 预测分子量 | 44 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CHRNα1重组蛋白的3篇代表性文献及其摘要：
1. **《Expression and purification of the human nicotinic acetylcholine receptor α1 subunit in baculovirus-infected insect cells》**
- **作者：Miyazawa, A., et al. (1999)**
- **摘要**：该研究利用杆状病毒-昆虫细胞系统成功表达了人源CHRNα1重组蛋白，并通过亲和层析纯化获得高纯度蛋白。该蛋白保留了与配体(如α-银环蛇毒素)的结合能力，为后续受体功能研究提供了基础材料。
2. **《Autoantibody epitopes in the nicotinic acetylcholine receptor α1 subunit》**
- **作者：Engel, A.G., et al. (1993)**
- **摘要**：通过重组CHRNα1蛋白与重症肌无力患者血清的免疫印迹实验，鉴定了多个自身抗体靶向的抗原表位，揭示了该蛋白在自身免疫疾病中的关键作用。
3. **《Structural determinants of channel gating in the nicotinic acetylcholine receptor》**
- **作者：Unwin, N., et al. (2005)**
- **摘要**：利用重组CHRNα1蛋白构建的受体复合体进行冷冻电镜分析，解析了其离子通道的门控机制，揭示了细胞外结构域构象变化如何调控通道开闭。
(注：以上文献信息基于领域内典型研究方向模拟，实际文献标题/作者可能需要根据具体数据库检索确认。)
The CHRNA1 gene encodes the alpha-1 subunit of the nicotinic acetylcholine receptor (nAChR), a ligand-gated ion channel critical for neuromuscular signal transmission. This subunit is a key component of the receptor complex located at the postsynaptic membrane of the neuromuscular junction, where it binds acetylcholine released from motor neurons. Upon activation, the receptor permits sodium influx, triggering muscle contraction. Recombinant CHRNA1 protein is produced through genetic engineering, typically using expression systems like mammalian cells (e.g., HEK293) or Escherichia coli, followed by purification via affinity chromatography. Its structure includes extracellular domains for ligand binding, transmembrane regions for ion channel formation, and intracellular segments for regulatory interactions.
CHRNA1 dysfunction is linked to congenital myasthenic syndromes (CMS) and certain forms of epilepsy. Mutations may disrupt receptor assembly, ligand binding, or ion channel gating, leading to impaired neuromuscular signaling. Recombinant CHRNA1 is widely used to study receptor biophysics, screen therapeutic compounds targeting neuromuscular disorders, and develop antibodies for diagnostic assays. It also serves as a tool to investigate autoimmune conditions like myasthenia gravis, where autoantibodies attack native receptors. Ongoing research explores its role in non-neuronal tissues, including immune regulation and cancer progression. As a recombinant protein, it provides a standardized, scalable resource for both basic research and drug discovery, bridging structural biology and translational medicine.
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