The IP Receptor is a class A rhodopsin-like G protein-coupled receptor that mediates the actions of prostaglandin I2 (PGI2). The C-terminal intracellular tail of the IP receptor undergoes isoprenylation and palmitoylation that results in anchoring of the tail to the plasma membrane. The IP receptor is expressed in platelets and vascular smooth muscle cells and in the aorta, lungs, heart, and kidneys. It signals through G proteins in a cell type- and expression-dependent manner and is involved in cardiovascular, inflammatory, and immune functions, as well as the pain response. An arginine-to-cysteine mutation at position 212 in the IP receptor inhibits its ability to activate adenylyl cyclase, which leads to increased platelet aggregation ex vivo and increases disease severity and the incidence of cardiovascular events in patients with a high risk of cardiovascular disease. The human IP receptor is N-terminally truncated by 28 amino acids compared with the murine receptor. Cayman’s IP Receptor (human) Polyclonal Antibody can be used for Western blot (WB). The antibody recognizes the IP receptor at approximately 42 kDa from human and mouse samples.
