Biological Background

The Glucagon-Like Peptide-2 Receptor (GLP-2R) is a class B GPCR predominantly expressed in the gastrointestinal tract, crucial for intestinal epithelial growth, mucosal integrity, and nutrient absorption. GLP-2R agonists such as teduglutide represent breakthrough therapies for short bowel syndrome and gastrointestinal disorders. β-arrestin recruitment provides G-protein-independent signaling essential for GPCR regulation.

This bioassay kit supports pharmaceutical companies developing GLP-2 receptor agonist therapies for gastrointestinal disorders, metabolic diseases, and intestinal failure. Applications include drug characterization, potency testing, and neutralizing antibody screening.

Eurofins DiscoverX's PathHunter® GLP2R kit offers a complete, ready-to-use solution for sensitive β-arrestin recruitment detection, supporting reliable GLP-2R drug characterization and potency testing.

Product Highlights
  • Functional GLP-2R β-arrestin recruitment assay using PathHunter® EFC technology for G-protein-independent GPCR signaling detection
  • Universal platform for measuring GLP-2R activation, ideal for characterizing agonists, antagonists, and neutralizing antibodies
  • Stoichiometric, non-amplified system providing improved sensitivity to antagonists and enhanced differentiation between partial and full agonists
  • Complete kit includes cells, detection reagents, plating media, control agonist (GLP-2), and 96-well assay plates for immediate use
  • Ideal for GLP2R drug characterization, potency testing, and neutralizing antibody screening

PathHunter CHO-K1 GLP2R Bioassay Assay Principle

PathHunter CHO-K1 GLP2R Bioassay Assay Principle

β-Arrestin Recruitment and PathHunter® Technology A. GLP-2R β-Arrestin Pathway Upon ligand binding (such as GLP-2, teduglutide, or other GLP-2R agonists), GLP-2R is phosphorylated by GPCR kinases, leading to β-arrestin-2 recruitment. This stoichiometric (1:1 receptor:ligand), non-amplified signal enhances sensitivity for detecting GLP-2R antagonists and differentiating between partial and full agonists compared to amplified second messenger assays. β-arrestin-2 binding terminates G-protein signaling and drives receptor internalization and desensitization. The receptor is then recycled or degraded. Analyzing the GLP-2R β-arrestin pathway allows fine-tuning of compound characterization, assessment of ligand bias versus G-protein pathways, and discrimination of full, super, and partial agonists.
B. PathHunter® Assay Technology. The PathHunter® GLP-2R assay uses Enzyme Fragment Complementation (EFC). GLP-2R is fused with a small enzyme donor fragment (ProLink™), and β-arrestin-2 carries the complementary enzyme acceptor fragment (EA). Upon GLP-2R activation by test compounds, β-arrestin-2 recruitment forces complementation of the enzyme fragments to reconstitute active β-galactosidase. This generates a chemiluminescent signal proportional to receptor activation. The β-arrestin recruitment assay complements cAMP and calcium assays, enabling comprehensive GLP-2R pharmacology profiling and expanding opportunities for novel GLP-2–based therapeutic development.