| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GCGR |
| Uniprot No | P47871 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-136aa |
| 氨基酸序列 | AQVMDFLFEKWKLYGDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPANT TANISCPWYLPWHHKVQHRFVFKRCGPDGQWVRGPRGQPWRDASQCQMDG EEIEVQKEVAK |
| 预测分子量 | 54 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条关于GCGR(胰高血糖素受体)重组蛋白的参考文献概览：
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1. **文献名称**：*Structure of the full-length glucagon class B G-protein-coupled receptor*
**作者**：Zhang, H. et al.
**摘要**：通过冷冻电镜技术解析全长GCGR的三维结构，揭示其与胰高血糖素结合的分子机制及跨膜信号传导途径，为靶向GCGR的药物设计提供结构基础。
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2. **文献名称**：*Expression and purification of recombinant human glucagon receptor for structural studies*
**作者**：Jazayeri, A. et al.
**摘要**：报道了一种优化哺乳动物细胞(HEK293)表达系统生产功能性GCGR重组蛋白的方法，结合亲和层析纯化技术获得高纯度蛋白，适用于X射线晶体学和功能研究。
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3. **文献名称**：*Development of a GCGR-based biosensor for high-throughput screening of antagonists*
**作者**：Yang, L. et al.
**摘要**：构建基于GCGR重组蛋白的荧光生物传感器，用于高通量筛选小分子拮抗剂，验证其对受体活性的抑制作用，为糖尿病治疗药物开发提供新工具。
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**备注**：以上文献为虚拟示例，实际研究中需查阅具体数据库(如PubMed、ScienceDirect)获取真实文献，并结合近年研究更新内容。
The glucagon receptor (GCGR) is a class B G protein-coupled receptor (GPCR) that plays a critical role in glucose homeostasis. It is primarily expressed in the liver, kidneys, and pancreas, where it binds glucagon, a peptide hormone released by pancreatic α-cells during fasting or hypoglycemia. Activation of GCGR triggers intracellular signaling cascades (e.g., cAMP-PKA pathway) to stimulate glycogenolysis and gluconeogenesis, thereby increasing blood glucose levels. Dysregulation of GCGR signaling is implicated in metabolic disorders, including type 2 diabetes and hyperglucagonemia, making it a therapeutic target for glycemic control.
Recombinant GCGR proteins are engineered versions of the receptor or its extracellular domains (ECDs), produced using heterologous expression systems like mammalian (e.g., CHO cells) or insect cells. These proteins retain functional or structural features of the native receptor and are essential tools for structural studies, ligand-binding assays, and drug discovery. For instance, GCGR ECD recombinant proteins have been used to resolve crystal structures of glucagon-bound complexes, revealing key interaction motifs that inform the design of antagonists or allosteric modulators.
Pharmaceutical interest in GCGR has grown with the development of dual or triple agonists targeting GCGR, GLP-1. and GIP receptors for obesity and diabetes. Recombinant GCGR proteins enable high-throughput screening of such therapeutics, while also aiding in understanding receptor dynamics, dimerization, and cross-talk with other signaling pathways. Challenges in production include maintaining proper post-translational modifications (e.g., glycosylation) and conformational stability. Advances in cryo-EM and protein engineering continue to refine GCGR recombinant tools, accelerating research into its pathophysiological roles and therapeutic potential.
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