Active • Host: HEK293 cells • AA: 26-138 • Tag: C-terminal His • MW: 14.42 kDa
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GIPR Extracellular Domain (human, recombinant; aa 26-138)

Item No. 42230

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
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, 5% trehalose, 5% mannitol, and 0.01% tween-80
UniProt Accession №
P48546
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $383

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    1 mg

    $2,489

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    Cayman Chemical
    Explore Obesity & Metabolic Disease Resources

    Discover high-quality research tools to investigate GLP-1 mechanisms and next-generation metabolic targets.

    OBESITY RESEARCH SOLUTIONS
    Product Description

    Glucose-dependent insulinotropic polypeptide receptor (GIPR) is a transmembrane glycoprotein hormone receptor and class B1 G protein-coupled receptor (GPCR).1 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.2,3 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 Gαs signaling.4,2,5 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.4 SNPs in GIPR are associated with type 2 diabetes.6 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.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Aksu, H., Demirbilek, A., and Uba, A.I. Insights into the structure and activation mechanism of some class B1 GPCR family members. Mol. Biol. Rep. 51(1), 966 (2024).

    2. Nauck, M.A., Quast, D.R., Wefers, J., et al. The evolving story of incretins (GIP and GLP-1) in metabolic and cardiovascular disease: A pathophysiological update. Diabetes Obes. Metab. 23 Suppl 3, 5-29 (2021).

    3. Whitaker, G.M., Lynn, F.C., McIntosh, C.H.S., et al. Regulation of GIP and GLP1 receptor cell surface expression by N-glycosylation and receptor heteromerization. PLoS One 7(3), e32675 (2012).

    4. Boer, G.A., Keenan, S.N., Miotto, P.M., et al. GIP receptor deletion in mice confers resistance to high-fat diet-induced obesity via alterations in energy expenditure and adipose tissue lipid metabolism. Am. J. Physiol. Endocrinol. Metab. 320(4), E835-E845 (2021).

    5. Rosenkilde, M.M., Lindquist, P., Kizilkaya, H.S., et al. GIP-derived GIP receptor antagonists - a review of their role in GIP receptor pharmacology. Peptides 177, 171212 (2024).

    6. Shalaby, S.M., Zidan, H.E., Shokry, A., et al. Association of incretin receptors genetic polymorphisms with type 2 diabetes mellitus in Egyptian patients. J. Gene Med. 19(9-10), e2973 (2017).