SLIGKv-NH2. A Potent Peptide Agonist of PAR2, Derived from PAR2 Auto-Ligand Sequence
Protease-activated receptors (PARs) 1-4 belong to the superfamily of G-protein-coupled receptors (GPCRs) that are self-activated by a tethered sequence exposed by proteolysis of an extracellular domain. PARs are activated by proteolysis in response to endogenous and exogenous proteases and can contribute to both cellular homeostasis and pathology.
In the case of PAR2, the exposed human peptide SLIGVK-NH2 remains tethered on the receptor and activates a primary binding site located on second loop of the receptor. As an obvious consequence of its activation mechanism, PAR2 is associated with pathologies with a strong protease release. The involvement of PAR2 in inflammatory diseases such as arthritis, lung inflammation (asthma), inflammatory bowel disease, sepsis, and pain disorders makes PAR2 an attractive target for drug intervention.
The extracellular N-terminus of PAR2 (46 residues long) contains a putative trypsin cleavage site R34 and S35, followed by LIGKv. The human-derived SLIGKv-NH2 is a small peptide that mimics the ligand binding properties of the tethered ligand exposed by proteolysis of the N-terminus from the natural receptor and hence, a significant tool used to study PAR2.
Alomone Labs is pleased to offer active and highly purified�SLIGKv-NH2 (GPS-100).
G-Protein Coupled Receptor Ligands; Proteinase-activated Receptor Ligands
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