Overview
- Peptide (C)KTRYSQKIGDDLS, corresponding to amino acid residues 200-212 of rat GCGR (Accession P30082). 1st extracellular loop.
- Rat kidney, rat and mouse liver lysates and human HepG2 liver carcinoma cell lysate (1:200-1:500).
Western blot analysis of rat kidney (lanes 1 and 5), rat liver (lanes 2 and 6), mouse liver (lanes 3 and 7) and human HepG2 liver carcinoma cell line (lanes 4 and 8) lysates:1-4. Anti-Glucagon Receptor (extracellular) Antibody (#AGR-024), (1:200).
5-8. Anti-Glucagon Receptor (extracellular) Antibody, preincubated with Glucagon Receptor (extracellular) Blocking Peptide (#BLP-GR024).
- Mouse brain sections (1:200).
The glucagon receptor (GCGR) is one of the 15 members of the secretin-like (class B) family of G-protein-coupled receptors (GPCRs) in humans. Glucagon is a highly conserved 29 amino acid protein processed from proglucagon by PC2 in pancreatic α-cells. The principal actions of glucagon involve regulation of metabolic pathways involved in glucose homeostasis1. Glucagon binding to the GCGR activates adenylyl cyclase through heterotrimeric Gs G proteins, leading to an increase in intracellular cAMP levels and subsequent activation of PKA signaling2.
The glucagon receptor is a 485-amino acid protein with a central core consisting of seven membrane-spanning domains, an extracellular N-terminus and a cytoplasmic C-terminal tail2.
Glucagon receptors are widely expressed in multiple tissues including the liver, brain, pancreas, heart, kidney, and smooth muscle cell in the gastrointestinal tract and peripheral vasculature1.
Abnormal glucagon signaling is associated with hyperglycemia in patients with type 2 diabetes3. Mice with homozygous null mutation of GCGR exhibit chronic hypoglycemia, extreme hyperglucagonemia, and α cell hyperplasia4. GCGR is a potential drug target for type 2 diabetes5.
