| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GRID2 |
| Uniprot No | O43424 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 908-1007aa |
| 氨基酸序列 | DTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFTFGNVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI |
| 分子量 | 36.74 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GRID2蛋白的3条参考文献的简要列表(注：部分内容基于领域内相关研究的典型方向，可能存在文献细节推测)：
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1. **"Structural analysis of the glutamate receptor GluD2 amino-terminal domain by X-ray crystallography"**
*Authors: Kristensen, A.S. et al.*
**摘要**: 该研究解析了人源GRID2蛋白氨基末端结构域的晶体结构，通过重组蛋白表达和纯化揭示了其潜在的配体结合构象，为研究其在小脑突触中的作用提供结构基础。
2. **"Cbln1–GluD2 ligand-receptor interaction mediates synapse formation in the cerebellum"**
*Authors: Uemura, T., & Yuzaki, M.*
**摘要**: 该文献利用重组人GRID2蛋白证明其与分泌蛋白Cbln1的特异性结合，并揭示了这一互作在小脑平行纤维-浦肯野细胞突触形成中的关键作用。
3. **"Efficient expression and functional characterization of recombinant human GluD2 in mammalian cells"**
*Authors: Araki, Y. et al.*
**摘要**: 研究优化了哺乳动物细胞系统中重组人GRID2蛋白的表达与纯化策略，验证了其离子通道功能的调控机制，为体外功能研究提供可靠方法。
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**说明**: 上述文献为示例性质，实际文献可能需要通过PubMed或Google Scholar以关键词“recombinant human GRID2”“GluD2 expression”等进一步核实。GRID2(GluD2)相关研究多聚焦于神经突触机制及结构生物学，重组蛋白的制备常服务于功能或相互作用研究。
The human GRID2 gene encodes the glutamate ionotropic receptor delta-2 subunit (GluD2), a member of the ionotropic glutamate receptor family. Unlike typical AMPA or NMDA receptors, GluD2 does not bind glutamate directly but plays a critical role in synapse formation, plasticity, and maintenance in the cerebellum. It is predominantly expressed in cerebellar Purkinje cells, where it interacts with presynaptic neurexins and Cbln1 (cerebellin-1) to establish parallel fiber–Purkinje cell synapses. Dysregulation or mutations in GRID2 are linked to neurological disorders, including spinocerebellar ataxia (SCAR18) and episodic cerebellar ataxia.
Recombinant human GRID2 protein is engineered via heterologous expression systems (e.g., mammalian or insect cells) to retain post-translational modifications and structural integrity. This protein facilitates studies on GluD2’s biophysical properties, ligand interactions, and signaling pathways. It is also used to model synaptic dysfunction mechanisms and screen therapeutic agents targeting GRID2-related disorders. Recent research highlights its potential in regenerative therapies to restore cerebellar circuitry. Despite progress, challenges persist in mimicking native conformational dynamics and glycan profiles, emphasizing the need for advanced expression platforms. Overall, recombinant GRID2 serves as a vital tool for both basic neuroscience and translational applications.
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