| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GRIN1 |
| Uniprot No | Q05586 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 834-938aa |
| 氨基酸序列 | EIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES |
| 预测分子量 | 18.0 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GRIN1(GluN1)重组蛋白的3篇参考文献概览：
---
1. **文献名称**：*Expression and Purification of the Recombinant GluN1/GluN2A NMDA Receptor Heterotetramer*
**作者**：Kazi, R., et al.
**摘要**：研究报道了人源NMDA受体GluN1/GluN2A异源四聚体的重组表达及纯化方法，利用昆虫细胞表达系统，结合亲和层析和尺寸排阻色谱技术获得高纯度蛋白，为后续结构功能研究提供基础。
---
2. **文献名称**：*Structural Insights into the Mechanism of GluN1-GluN2A NMDA Receptor Assembly*
**作者**：Lee, C.H., et al.
**摘要**：通过冷冻电镜解析了重组GluN1/GluN2A受体蛋白的三维结构，揭示了亚基间相互作用的关键位点，阐明了NMDA受体组装及门控机制的结构基础。
---
3. **文献名称**：*Functional Characterization of Recombinant GluN1/GluN2D NMDA Receptors in Xenopus Oocytes*
**作者**：Vicini, S., et al.
**摘要**：在非洲爪蟾卵母细胞中重组表达GluN1与GluN2D亚基，通过电生理技术分析其药理学特性及通道动力学，证实不同亚基组合对受体功能的特异性调控。
---
(注：上述文献信息为示例，实际引用需以具体数据库检索结果为准。)
GRIN1 recombinant protein is derived from the GRIN1 gene, which encodes the GluN1 subunit of the N-methyl-D-aspartate (NMDA) receptor, a critical ligand-gated ion channel in the central nervous system. NMDA receptors are heterotetrameric complexes typically composed of two GluN1 subunits and two GluN2 or GluN3 subunits. The GluN1 subunit, produced by the GRIN1 gene, is essential for receptor assembly and function, serving as the obligatory component for all NMDA receptor configurations. It contains binding sites for glycine (or D-serine), a co-agonist required for channel activation, and plays a pivotal role in synaptic plasticity, learning, and memory.
Recombinant GRIN1 proteins are generated using biotechnological methods, such as expression in mammalian, insect, or bacterial cell systems, followed by purification. These proteins enable researchers to study the structural and functional properties of NMDA receptors in vitro. For instance, they are used to investigate receptor-ligand interactions, ion channel gating mechanisms, and the impact of genetic mutations linked to neurological disorders like epilepsy, schizophrenia, and Alzheimer’s disease. Mutations in GRIN1 are associated with altered receptor activity, leading to excitotoxicity or hypoactivity, which underscores its pathophysiological relevance.
The development of GRIN1 recombinant proteins has also advanced drug discovery, particularly in screening compounds targeting NMDA receptors for therapeutic applications. Structural studies using cryo-electron microscopy or X-ray crystallography often rely on purified recombinant subunits to resolve receptor architecture. However, challenges remain in replicating native post-translational modifications or subunit interactions in vitro, necessitating optimized expression systems. Overall, GRIN1 recombinant proteins serve as indispensable tools for deciphering NMDA receptor biology and developing treatments for neurological and psychiatric conditions.
×
