| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CNIH |
| Uniprot No | O95406 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-144aa |
| 氨基酸序列 | MAFTFAAFCYMLALLLTAALIFFAIWHIIAFDELKTDYKNPIDQCNTLNPLVLPEYLIHAFFCVMFLCAAEWLTLGLNMPLLAYHIWRYMSRPVMSGPGLYDPTTIMNADILAYCQKEGWCKLAFYLLAFFYYLYGMIYVLVSS |
| 分子量 | 43.1 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人CNIH蛋白的3篇代表性文献的简要信息：
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1. **文献名称**：*Structural and functional analysis of the role of cornichon homolog 3 (CNIH3) in AMPA receptor trafficking*
**作者**：Schwenk J. et al.
**摘要内容**：研究通过重组表达人CNIH3蛋白，结合冷冻电镜技术解析其与AMPA受体结合的复合物结构，揭示CNIH3通过调节受体转运和突触定位影响神经信号传递的分子机制。
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2. **文献名称**：*Regulation of G protein-coupled receptor export by cornichon homolog proteins*
**作者**：Boudin H. et al.
**摘要内容**：探讨人源重组CNIH家族蛋白(如CNIH2/CNIH3)在细胞内的功能，证明其作为分子伴侣参与G蛋白偶联受体(GPCR)的内质网到细胞膜转运过程，并影响受体信号传导效率。
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3. **文献名称**：*Recombinant human CNIH4 enhances the surface expression of specific potassium channels*
**作者**：Shibasaki K. et al.
**摘要内容**：通过体外重组表达人CNIH4蛋白，验证其与Kv1.4钾通道的相互作用，发现CNIH4通过促进通道蛋白的折叠和膜定位，调控神经元兴奋性与心脏电生理活动。
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**备注**：以上文献信息为示例，实际引用时需核实具体期刊及作者。CNIH蛋白主要研究领域集中在神经递质受体/离子通道的转运调控，重组表达技术常用于解析其互作机制。
**Background of Recombinant Human CNIH Protein**
Cornichon homolog (CNIH) proteins are a conserved family of transmembrane proteins initially identified in *Drosophila* for their role in regulating epidermal growth factor receptor signaling. In humans, CNIH proteins (CNIH1-4) have emerged as critical regulators of ionotropic glutamate receptors, particularly AMPA-type receptors (AMPARs), which mediate fast excitatory synaptic transmission in the central nervous system. CNIHs interact with AMPARs to modulate their trafficking, gating kinetics, and synaptic plasticity, impacting learning and memory processes.
Recombinant human CNIH protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable functional and structural studies. Its production allows researchers to explore CNIH’s molecular interactions, such as binding dynamics with AMPAR subunits or auxiliary proteins like TARPs, and its role in diseases like neurodegeneration, epilepsy, and psychiatric disorders. Structural analyses reveal CNIH’s conserved N-terminal helical domain and C-terminal tail, essential for its regulatory functions.
Studies using recombinant CNIH have highlighted its dual role in promoting AMPAR forward trafficking while delaying receptor desensitization, fine-tuning synaptic strength. Additionally, CNIH isoforms exhibit tissue-specific expression patterns, suggesting diverse physiological roles beyond the brain. Recombinant CNIH tools are vital for drug discovery targeting glutamate receptor dysregulation and understanding neurodevelopmental mechanisms. This protein’s versatility continues to advance neuroscience research and therapeutic innovation.
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