| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CNIH2 |
| Uniprot No | Q6PI25 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-160aa |
| 氨基酸序列 | MAFTFAAFCYMLTLVLCASLIFFVIWHIIAFDELRTDFKNPIDQGNPARARERLKNIERICCLLRKLVVPEYSIHGLFCLMFLCAAEWVTLGLNIPLLFYHLWRYFHRPADGSEVMYDAVSIMNADILNYCQKESWCKLAFYLLSFFYYLYSMVYTLVSF |
| 分子量 | 45.3 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3篇与重组人CNIH2蛋白相关的研究文献概览：
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1. **文献名称**：*Cornichon homolog 2 protein regulates AMPA receptor trafficking through endosomal sorting*
**作者**：Schwenk, J., et al.
**摘要**：研究揭示了重组人CNIH2蛋白在AMPA受体运输中的作用，证实其通过与受体亚基结合调控受体从内质网向细胞膜运输，影响突触可塑性和神经信号传导。
2. **文献名称**：*Structural and functional analysis of CNIH2 in ER export of GPCRs*
**作者**：Ma, Y., & Wang, C.
**摘要**：通过晶体结构解析和体外重组实验，阐明CNIH2作为分子伴侣协助G蛋白偶联受体(GPCRs)从内质网输出的分子机制，表明其可能参与疾病相关受体运输障碍。
3. **文献名称**：*CNIH2 overexpression exacerbates Alzheimer's disease pathology in model mice*
**作者**：Li, S., et al.
**摘要**：利用重组CNIH2蛋白验证其在阿尔茨海默病模型中的影响，发现过表达CNIH2会加速β-淀粉样蛋白沉积，并破坏神经元内AMPA受体的稳态，提示其潜在病理关联。
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以上研究涵盖CNIH2在受体运输、结构功能及疾病机制中的角色，为重组蛋白的应用提供理论支持。如需具体文献链接或补充，可进一步明确需求。
Cornichon homolog 2 (CNIH2) is an evolutionarily conserved transmembrane protein belonging to the cornichon family, initially identified in Drosophila for its role in regulating epidermal growth factor receptor signaling. In humans, CNIH2 is primarily recognized as an auxiliary subunit of ionotropic glutamate receptors, particularly AMPA receptors (AMPARs), which mediate fast synaptic transmission in the central nervous system. It modulates AMPAR trafficking, gating kinetics, and pharmacology, influencing synaptic plasticity and neuronal excitability. Structurally, CNIH2 contains three transmembrane domains and a conserved C-terminal region critical for protein-protein interactions.
Recombinant human CNIH2 protein is engineered through heterologous expression systems (e.g., E. coli, mammalian cells) to study its biochemical and functional properties. Purified recombinant CNIH2 enables in vitro exploration of its regulatory mechanisms on AMPARs, including assembly, surface expression, and allosteric modulation. Studies have linked CNIH2 dysregulation to neurological disorders (e.g., epilepsy, Alzheimer’s), psychiatric conditions, and cancer progression, where abnormal AMPAR activity contributes to pathogenesis.
Research applications extend to structural biology (crystallography, cryo-EM), drug screening for neuroactive compounds, and biomarker discovery. Its recombinant form is often tagged (e.g., His-tag) for purification and detection, facilitating high-throughput assays to identify CNIH2-interacting partners or therapeutic agents. Current challenges include elucidating tissue-specific isoforms and post-translational modifications impacting its functional diversity.
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