Glucagon Receptor Extracellular Domain (human, recombinant)

Glucagon receptor (GCGR) is a transmembrane glycoprotein and class B G protein-coupled receptor (GPCR).^1,2 It is composed of an N-terminal extracellular domain required for ligand binding, seven transmembrane domains, and a C-terminal intracellular domain.³ It is expressed primarily in the liver and kidney but is also found in a variety of other areas, including adipose tissue and the pancreas, heart, gastrointestinal tract, and brain.^3,2,1 Under hypoglycemic conditions, GCGR is activated by increased levels of glucagon and induces Gα_s signaling, which initiates the transcription of enzymes involved in gluconeogenesis and the activation of enzymes involved in glycogenolysis to increase blood levels of glucose.¹ A glycine-to-serine mutation at position 40 of GCGR (GCGR^G40S) decreases its affinity to glucagon and is associated with type 2 diabetes.⁴ Inactivating mutations in GCGR are associated with pancreatic α-cell hyperplasia, hyperaminoacidemia, and hyperglucagonemia but not hypoglycemia.^1,5,6 Cayman's Glucagon Receptor Extracellular Domain (human, recombinant) protein can be used for binding assays. This protein consists of 122 amino acids, has a calculated molecular weight of 14.5 kDa, and a predicted N-terminus of Ala26 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 36 kDa due to glycosylation.

WARNING This product is not for human or veterinary use.

1. Janah, L., Kjeldsen, S., Galsgaard, K.D., et al. Glucagon receptor signaling and glucagon resistance. Int. J. Mol. Sci. 20(13), 3314 (2019).

2. Authier, F., and Desbuquois, B. Glucagon receptors. Cell Mol. Life Sci. 65(12), 1880-1899 (2008).

3. Mayo, K.E., Miller, L.J., Bataille, D., et al. International Union of Pharmacology. XXXV. The glucagon receptor family. Pharmacol. Rev. 55(1), 167-194 (2033).

4. Hager, J., Hansen, L., Vaisse, C., et al. A missense mutation in the glucagon receptor gene is associated with non-insulin-dependent diabetes mellitus. Nat. Genet. 9(3), 299-304 (1995).

5. Larger, E., Wewer Albrechtsen, N.J., Hansen, L.H., et al. Pancreatic α-cell hyperplasia and hyperglucagonemia due to a glucagon receptor splice mutation. Endocrinol. Diabetes Metab. Case Rep. (2016).

6. Zhou, C., Dhall, D., Missen, N.N., et al. Homozygous P86S mutation of the human glucagon receptor is associated with hyperglucagonemia, α cell hyperplasia, and islet cell tumor. Pancreas 38(8), 941-946 (2009).