Recombinant Human IGF2R

Background

The insulin-like growth factor 2 receptor (IGF2R) is a multi-functional transmembrane protein primarily known for binding and internalizing insulin-like growth factor 2 (IGF-2). Unlike the insulin-like growth factor 1 receptor (IGF1R), which signals to promote cell proliferation and survival, IGF2R generally acts to limit the bioavailability of IGF-2 and is therefore considered a negative regulator of growth. IGF2R also binds other ligands, including mannose-6-phosphate-tagged proteins, such as lysosomal enzymes, which it transports from the Golgi to lysosomes. This receptor is widely expressed in mammalian tissues and has important roles in development, cellular signaling, and protein trafficking. IGF2R is unique in its signaling capacity, as it lacks intrinsic tyrosine kinase activity. It operates mainly through ligand sequestration, ligand degradation, and the modulation of signaling pathways indirectly by reducing IGF-2 interactions with IGF1R. IGF2R’s role in growth regulation and its involvement in diseases, particularly cancer, has made it a focal point in biomedical research.