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首页 >> 实验室试剂 >> 生命科学 >> Recombinant Human GIPR Protein
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  • 所属类别:实验室试剂
  • 产品品牌:阿拉丁
  • 价格区间:1万以上
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阿拉丁rp188259


Recombinant Human GIPR Protein

别名重组人GIPR蛋白 | 重组人胃抑制多肽受体蛋白
英文别名gastric inhibitory polypeptide receptor | GIPR | GIP-R | Glucose-dependent insulinotropic polypeptide receptor | MGC126722 | PGQTL2
规格或纯度无动物源, 无载体, ≥95%(SDS-PAGE), 见COA
生化机理Human Gastric Inhibitory Polypeptide Receptor (GIPR) is a transmembrane G protein coupled receptor that is mainly found in beta-cells within the pancreas. GIPR has 117 aa extracellular domain on its N-terminus, a central region consisting of seven transmembrane domains and a 68 aa C-terminal cytoplasmic domain that is responsible for intracellular transduction with the G-Protein. GIPR has three known isoforms produced by alternative splicing. The extracellular domain of human GIPR shows 76.3% and 81.2% amino acid identity with mouse and rat homolog, respectively. When originally discovered, GIPR was thought to have a role of inhibiting the secretion of gastrin and gastric acid. However, it was subsequently discovered that GIPR's main function was to stimulate the release of insulin in the presence of elevated blood glucose levels. GIPR has been found to bind to glucagon-like peptide-1 (GIP) and cascades downstream to release insulin. GIP and its receptor (GIPR) are of high pharmacological interest, since expression of GIPR are found in different organs and systems, especially in identification and design of new molecules for the treatment of diabetes mellitus and obesity. GIPR has also been shown to have an indirect relation with bone health and density. Mouse overexpressing GIP and GIPR had increased levels of osteoblasts and an overall decrease in age-related bone loss, while mice with GIPR knockout showed a decrease in overall bone mass and a higher level of compromised bone mass. Targeted Radionuclide Therapy (TRT) against GIPR positive cancer cells showed a significant increase of cell cycle arrest, specifically at the G2 and M phase, along with extensive DNA damage. Post-translational: N-glycosylation is required for cell surface expression and lengthens receptor half-life by preventing degradation in the ER.
生物活性Testing in progress


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