GIPR Extracellular Domain (human, recombinant, aa 26-138)

Glucose-dependent insulinotropic polypeptide receptor (GIPR) is a transmembrane glycoprotein hormone receptor and class B1 G protein-coupled receptor (GPCR). It is composed of an N-terminal extracellular domain required for ligand binding, seven transmembrane domains, and a C-terminal intracellular domain. GIPR is expressed in adipose tissue and the pancreas, gut, heart, pituitary gland, adrenal cortex, and brain and localizes to the plasma membrane. It is involved in insulin and glucagon secretion, bone remodeling, and lipid metabolism, is activated by the endogenous ligands GIP (1-42) and GIP (1-30) amide, and induces primarily Galphas signaling. Knockout of GIPR increases lipolysis in white adipose tissue and reduces body weight gain and fat mass in a mouse model of obesity induced by a high-fat diet. SNPs in GIPR are associated with type 2 diabetes. Cayman's GIPR Extracellular Domain (human, recombinant, aa 26-138) protein can be used for binding assays. This protein consists of 124 amino acids, has a calculated molecular weight of 14.42 kDa, and a predicted N-terminus of Gly26 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 25.7 kDa due to glycosylation.Synonyms: Gastric Inhibitory Polypeptide Receptor, Glucose-dependent Insulinotropic Polypeptide Receptor. Purity: >95% as determined by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg determined by the LAL endotoxin assay. Source: Active recombinant human C-terminal His-tagged GIPR extracellular domain expressed in HEK293 cells. Amino Acids: 26-138. MW: 14.42 kDa. Formulation: (Request formulation change), Lyophilized from sterile PBS, pH 7.4. UniProt Accession No: P48546.