Proteinase-Activated Receptor 1 (F2R) Antibody

Background

Proteinase-Activated Receptor 1 (F2R), or PAR1, is a G protein-coupled receptor activated by thrombin, a serine protease involved in coagulation and cellular signaling. PAR1 activation occurs through proteolytic cleavage of its N-terminal domain, exposing a tethered ligand that activates the receptor. PAR1 couples to Gq, Gi, and G12/13 proteins, triggering diverse signaling pathways, including phospholipase C (PLC), MAPK, and Rho-mediated pathways. PAR1 is widely expressed in endothelial cells, platelets, smooth muscle cells, and neurons, where it regulates thrombosis, inflammation, vascular permeability, and tissue repair. In platelets, PAR1 activation promotes aggregation and thrombus formation, while in endothelial cells, it modulates vascular integrity and inflammation. Dysregulation of PAR1 contributes to thrombotic disorders, cancer progression, and inflammatory diseases. PAR1 antagonists, such as vorapaxar, are clinically used to reduce thrombotic events in patients with cardiovascular disease. Targeting PAR1 offers therapeutic benefits in thrombosis, cancer, and inflammatory vascular disorders.