Recombinant Human PAR2

Background

Proteinase-Activated Receptor 2 (F2RL1), also known as PAR2, is a G protein-coupled receptor (GPCR) activated by the cleavage of its N-terminal domain by serine proteases, such as trypsin and mast cell tryptase. PAR2 is widely expressed in various tissues, including endothelial cells, platelets, smooth muscle, and immune cells, where it regulates inflammatory responses, cell migration, and pain perception. Upon activation, F2RL1 couples to Gq, Gi, and G12/13 proteins, stimulating phospholipase C (PLC), MAPK, and Rho signaling pathways. These pathways lead to increased intracellular calcium, cell contraction, and gene expression associated with inflammation. F2RL1 plays a role in immune cell recruitment during allergic reactions, wound healing, and tissue remodeling. Dysregulation of F2RL1 has been implicated in inflammatory diseases, cancer metastasis, and pain disorders. PAR2 antagonists are being developed for therapeutic applications in conditions like asthma, chronic pain, and cancer, by modulating its pro-inflammatory effects and enhancing tissue repair.