| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHRNa7 |
| Uniprot No | P36544 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-230aa |
| 氨基酸序列 | GEFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPPGIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPGKRSERFYECCKEPYPDVTFTVTMRRRT |
| 预测分子量 | 30.4 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CHRNa7重组蛋白的虚构参考文献示例，内容基于常见研究方向概括：
1. **文献名称**：*Expression and Purification of Recombinant Human α7 Nicotinic Acetylcholine Receptor in HEK293 Cells*
**作者**：Smith J, et al.
**摘要**：研究报道了在HEK293哺乳动物细胞中高效表达和纯化功能性CHRNa7重组蛋白的方法，通过电生理实验验证其离子通道活性，为受体功能研究提供工具。
2. **文献名称**：*Structural Insights into the α7 Nicotinic Receptor Ligand Binding Domain via Recombinant Protein Crystallography*
**作者**：Lee S, et al.
**摘要**：利用重组CHRNa7配体结合域蛋白进行X射线晶体学研究，揭示了乙酰胆碱结合位点的三维结构，阐明其与激动剂/拮抗剂相互作用的分子机制。
3. **文献名称**：*CHRNa7 Recombinant Protein Ameliorates Cognitive Deficits in Alzheimer's Disease Mouse Models*
**作者**：Wang Y, et al.
**摘要**：通过在阿尔茨海默病模型小鼠中注射重组CHRNa7蛋白，发现其可激活胆碱能抗炎通路，改善突触可塑性和认知功能，提示治疗潜力。
4. **文献名称**：*In Vitro Assembly of Functional α7 Nicotinic Receptors Using Recombinant Subunits*
**作者**：Garcia R, et al.
**摘要**：开发了一种基于大肠杆菌表达系统重组生产CHRNa7亚基的技术，结合脂质体重组技术成功复受体功能，用于高通量药物筛选。
(注：以上文献为示例，实际研究中需检索真实数据库获取准确信息。)
**Background of CHRNa7 Recombinant Protein**
The α7 nicotinic acetylcholine receptor (α7 nAChR), encoded by the *CHRNA7* gene, is a ligand-gated ion channel predominantly expressed in the central nervous system, immune cells, and peripheral tissues. It plays a critical role in modulating synaptic transmission, neurodevelopment, and inflammatory responses. Structurally, it forms a homomeric pentameric complex, distinguishing it from other heteromeric nAChRs. The receptor is highly permeable to calcium ions and is implicated in cognitive functions, including learning and memory. Dysregulation of α7 nAChR has been linked to neuropsychiatric disorders (e.g., schizophrenia, Alzheimer’s disease) and chronic inflammatory conditions.
Recombinant CHRNA7 protein is engineered in vitro to study its biological functions, ligand interactions, and therapeutic potential. Produced via heterologous expression systems (e.g., mammalian, insect, or bacterial cells), it enables structural analysis, drug screening, and mechanistic studies. Challenges in producing functional α7 nAChR recombinants arise from its complex pentameric assembly and low solubility. Advances in protein engineering, such as fusion tags or chaperone co-expression, have improved stability and yield.
Research on α7 nAChR recombinant proteins is pivotal for developing targeted therapies. Agonists like GTS-21 or positive allosteric modulators aim to enhance cholinergic signaling in cognitive disorders. Additionally, its role in the “cholinergic anti-inflammatory pathway” highlights potential applications in treating sepsis or autoimmune diseases. However, limitations persist, including receptor desensitization and off-target effects. Recent studies also explore its interaction with the *CHRFAM7A* hybrid gene, unique to primates, which may influence receptor function and drug responses.
Overall, CHRNA7 recombinant proteins serve as essential tools for unraveling the receptor’s pathophysiology and advancing precision medicine in neurology and immunology.
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