PAR2 Protein, Human (sf9, Flag, His)

PAR2 is a G protein-coupled receptor for trypsin and trypsin-like enzymes, functioning through activation of pathways including PLC, intracellular calcium, MAPK, NF-kappaB, and Rho. It can be transactivated by cleaved PAR1 and modulates inflammatory responses, immunity, and acts as a sensor for infection-related proteases, generally promoting inflammation. PAR2 synergizes with TLR4/TLR2 in inflammation and regulates TLR3 signaling. It protects endothelial barrier integrity (involving factor X) and regulates neutrophil extravasation (potentially via PRTN3 cleavage). In airways, it exhibits both bronchoprotective and barrier-disrupting effects (via E-cadherin interruption). PAR2 mediates hypotension through vasodilation and associates with GNAQ/GNA11 but not certain G(i) subunits (though G(i)-alpha signaling was reported). As a class B receptor, it internalizes with arrestin. It inhibits TNF-α-induced JNK phosphorylation via GNAQ/GNA11 and mediates RELA Ser-536 phosphorylation (largely G protein-independent). PAR2 drives migration/chemotaxis via β-arrestin scaffolds and recruits leukocytes to inflammation sites. It enhances phagocytosis, bacterial killing, and antiviral responses, implicated in inflammatory/autoimmune diseases. By similarity: proposed to mediate pro-inflammatory/fibrotic fibroblast responses triggered by factor Xa; demonstrated function (PubMed:22409427): mediates endothelial barrier-protective signaling via factor Xa.