| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GIPR |
| Uniprot No | P48546 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-138aa |
| 氨基酸序列 | RAETGSKGQTAGELYQRWERYRRECQETLAAAEPPSGLACNGSFDMYVCW DYAAPNATARASCPWYLPWHHHVAAGFVLRQCGSDGQWGLWRDHTQCENP EKNEAFLDQRLILERLQ |
| 预测分子量 | 19 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GIPR重组蛋白的3篇文献概述(基于假设性研究内容)：
1. **《Structural insights into GIPR activation by cryo-EM》**
- **作者**: Zhang Y. et al.
- **摘要**: 通过冷冻电镜技术解析了GIPR与内源性配体GIP结合的复合物结构，揭示了受体跨膜结构域的构象变化及G蛋白偶联机制，为设计靶向GIPR的糖尿病药物提供结构基础。
2. **《Dual GIPR/GLP-1R agonists promote weight loss via synergistic metabolic effects》**
- **作者**: Finan B. et al.
- **摘要**: 研究开发了一种重组双靶点激动剂，可同时激活GIPR和GLP-1R，显著改善肥胖模型小鼠的糖代谢并减少脂肪积累，表明GIPR信号在代谢调控中具有潜在治疗价值。
3. **《GIPR signaling bias toward β-arrestin in pancreatic β-cells》**
- **作者**: Jiang L. et al.
- **摘要**: 利用重组GIPR蛋白及细胞模型，发现GIPR激活后优先招募β-arrestin而非G蛋白通路，这种信号偏好可能影响胰岛素分泌的持续性，为优化GIPR靶向药物提供新方向。
4. **《Expression and functional characterization of recombinant GIPR in HEK293 cells》**
- **作者**: Kumar S. et al.
- **摘要**: 报道了在HEK293细胞中高效表达功能性GIPR重组蛋白的方法，并验证其配体结合活性及下游cAMP信号响应，为体外研究GIPR功能提供可靠模型。
(注：上述文献为假设性示例，实际文献需通过数据库如PubMed检索确认。)
The glucose-dependent insulinotropic polypeptide receptor (GIPR) is a class B G protein-coupled receptor (GPCR) that plays a critical role in metabolic regulation. It is activated by glucose-dependent insulinotropic polypeptide (GIP), an incretin hormone secreted by intestinal K-cells in response to nutrient intake. Structurally, GIPR consists of seven transmembrane domains and is expressed in various tissues, including pancreatic β-cells, adipose tissue, and the gastrointestinal tract. Its primary function involves enhancing glucose-stimulated insulin secretion, promoting lipid storage in adipocytes, and modulating bone metabolism. Dysregulation of GIPR signaling has been implicated in metabolic disorders such as type 2 diabetes and obesity.
Recombinant GIPR proteins are engineered in vitro using expression systems like mammalian cells or bacteria to study receptor-ligand interactions, signaling pathways, and therapeutic potential. These proteins retain key functional domains, enabling researchers to investigate GIPR's role in physiology and disease. For example, GIPR agonists and antagonists are being explored for their ability to modulate insulin secretion or adipose tissue metabolism. Recent studies also highlight its crosstalk with the glucagon-like peptide-1 receptor (GLP-1R), inspiring combination therapies for diabetes. However, GIPR's dual role in both promoting and mitigating metabolic complications (e.g., conflicting effects on fat accumulation) remains a research focus. Advances in recombinant technology, including cryo-EM structural analysis, have improved understanding of GIPR activation mechanisms, aiding the design of biased ligands to optimize therapeutic outcomes.
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