| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLP1R |
| Uniprot No | P43220 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-145aa |
| 氨基酸序列 | MKHHHHHHAS RPQGATVSLW ETVQKWREYR RQCQRSLTED PPPATDLFCN RTFDEYACWP DGEPGSFVNV SCPWYLPWAS SVPQGHVYRF CTAEGLWLQK DNSSLPWRDL SECEESKRGE RSSPEEQLLF LY |
| 预测分子量 | 16 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GLP1R重组蛋白研究的3篇代表性文献示例(文献名称与作者为虚构示例，仅用于格式参考)：
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1. **文献名称**: *Structural Basis of GLP-1 Receptor Activation by a Small Molecule Agonist*
**作者**: Zhang, Y. et al.
**摘要**: 通过冷冻电镜技术解析了GLP1R与重组蛋白配体复合物的三维结构，揭示了小分子激动剂结合受体跨膜结构域并激活下游信号通路的分子机制，为糖尿病药物设计提供结构基础。
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2. **文献名称**: *Recombinant GLP-1R Fusion Protein Enhances Insulin Secretion in β-Cells*
**作者**: Smith, J. & Brown, K.
**摘要**: 研究开发了一种重组GLP1R融合蛋白，证明其可通过增强受体稳定性与配体结合能力，显著促进β细胞胰岛素分泌，并在动物模型中改善血糖控制。
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3. **文献名称**: *Targeting GLP1R for Obesity Therapy: A Recombinant Long-Acting Agonist*
**作者**: Lee, H. et al.
**摘要**: 报道了一种长效重组GLP1R激动剂的设计与功能评价，通过延长半衰期和优化受体亲和力，在肥胖模型中有效抑制食欲并减轻体重，具有潜在临床转化价值。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词“GLP1R recombinant protein structure/therapy/agonist”获取近年研究。
The glucagon-like peptide-1 receptor (GLP1R) is a class B G protein-coupled receptor (GPCR) that plays a critical role in glucose metabolism and insulin secretion. It is primarily expressed in pancreatic β-cells, the gastrointestinal tract, and the central nervous system. GLP1R is activated by its endogenous ligand, glucagon-like peptide-1 (GLP-1), a hormone released from intestinal L-cells in response to nutrient intake. Activation of GLP1R triggers intracellular signaling pathways, including cAMP-PKA and MAPK, which enhance glucose-dependent insulin secretion, suppress glucagon release, slow gastric emptying, and promote satiety. These actions make GLP1R a key therapeutic target for type 2 diabetes and obesity.
Recombinant GLP1R proteins are engineered versions of the receptor produced in heterologous expression systems (e.g., mammalian, insect, or bacterial cells) for research and drug development. They retain the receptor's functional domains, including the extracellular ligand-binding region, transmembrane helices, and intracellular signaling motifs. Recombinant GLP1R enables structural studies (e.g., X-ray crystallography, cryo-EM) to elucidate ligand-receptor interaction mechanisms and supports high-throughput screening of GLP-1 analogs or small-molecule agonists. Drugs like exenatide and liraglutide, which mimic GLP-1. rely on GLP1R activation for their glucose-lowering effects.
Recent advances in recombinant protein technology have improved the stability and solubility of GLP1R, facilitating its use in biophysical assays and antibody development. Challenges remain in maintaining native receptor conformation and post-translational modifications (e.g., glycosylation) during production. Nonetheless, recombinant GLP1R remains indispensable for understanding receptor pharmacology and designing next-generation therapies targeting metabolic disorders.
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