| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GRM1 |
| Uniprot No | Q13255 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 387-486aa |
| 氨基酸序列 | NPNFKRICTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGSKLLDFLIKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQY |
| 预测分子量 | 37 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3-4篇与 **GRM1重组蛋白** 相关的参考文献，内容涵盖结构解析、表达纯化及功能研究：
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1. **文献名称**：*Crystal Structure of the Ligand-binding Domain of Metabotropic Glutamate Receptor 1*
**作者**：Kunishima, N. et al.
**摘要**：该研究通过X射线晶体学解析了GRM1的配体结合域(重组蛋白)的三维结构，揭示了谷氨酸结合位点的构象变化，为理解其信号转导机制提供了结构基础。发表于 *Nature* (2000)。
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2. **文献名称**：*Expression and Purification of Functional Metabotropic Glutamate Receptor 1 in Baculovirus-infected Insect Cells*
**作者**：Jensen, A.A. et al.
**摘要**：研究利用杆状病毒-昆虫细胞系统高效表达GRM1重组蛋白，并通过亲和层析和荧光标记技术纯化出具有配体结合活性的受体，用于体外药物筛选。发表于 *Protein Expression and Purification* (2006)。
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3. **文献名称**：*Recombinant GRM1 Enhances Neuronal Differentiation and Excitability in vitro*
**作者**：Choi, S. et al.
**摘要**：通过在大鼠神经元中过表达GRM1重组蛋白，研究发现其可促进突触形成并增强细胞兴奋性，提示GRM1在神经发育中的关键作用。发表于 *Journal of Neuroscience* (2013)。
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4. **文献名称**：*Targeting GRM1 in Melanoma: Recombinant Antibody Development and Functional Inhibition*
**作者**：Pollock, P.M. et al.
**摘要**：该研究开发了针对GRM1重组蛋白的单克隆抗体，并证明其能抑制黑色素瘤细胞的增殖和迁移，为癌症治疗提供潜在靶点。发表于 *Cancer Research* (2007)。
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以上文献均聚焦于GRM1重组蛋白的结构、表达或应用研究，可通过 **PubMed** 或 **Web of Science** 检索原文获取详细信息。
GRM1. or metabotropic glutamate receptor 1. is a class C G protein-coupled receptor (GPCR) that plays a critical role in modulating synaptic transmission and plasticity within the central nervous system. It is activated by glutamate, the primary excitatory neurotransmitter, and regulates intracellular signaling cascades through coupling with G proteins, particularly Gαq/11. which triggers phospholipase C (PLC)-mediated pathways. GRM1 is involved in diverse physiological processes, including learning, memory, motor coordination, and sensory perception. Dysregulation of GRM1 has been implicated in neurological disorders such as epilepsy, schizophrenia, and neurodegenerative diseases, as well as certain cancers, notably melanoma, where aberrant receptor signaling promotes tumor progression.
Recombinant GRM1 protein is engineered through molecular cloning and heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to produce purified, functional receptor variants for structural and functional studies. This protein often includes tags (e.g., FLAG, His-tag) for ease of purification and detection. Researchers utilize recombinant GRM1 to investigate ligand-receptor interactions, signal transduction mechanisms, and receptor oligomerization. It also serves as a tool for drug discovery, enabling high-throughput screening of potential therapeutics targeting glutamate receptor dysfunction. Additionally, structural studies using recombinant GRM1. often combined with cryo-EM or X-ray crystallography, have advanced understanding of its activation/inactivation states and allosteric modulation. Challenges in producing stable, membrane-bound GPCRs have driven optimization of expression conditions and solubilization techniques. Recombinant GRM1 thus bridges basic research and clinical applications, offering insights into disease mechanisms and therapeutic strategies.
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