Formylpeptide Receptor 1 Antibodies

Formyl peptide receptor 1 (FPR1), encoded by FPR1, is a class A G protein-coupled receptor that detects N-formylated peptides derived from bacteria and damaged mitochondria. The bacterial tripeptide N-formyl-Met-Leu-Phe (fMLF) is a prototypical FPR1 agonist widely used in experimental studies. FPR1 couples predominantly to Gi/o, activating pathways that control intracellular calcium mobilization and directed cell migration. It is highly expressed on neutrophils and is also found on monocytes and macrophages. In neutrophils, FPR1 activation promotes recruitment to sites of infection or tissue injury and can trigger degranulation and reactive oxygen species production. Agonist stimulation induces phosphorylation of the receptor’s C-terminal tail, contributing to desensitization, while the fate of the internalized receptor depends on the ligand. In experimental systems, fMLF promotes receptor recycling, whereas the related peptide fMLFC can direct FPR1 toward lysosomal degradation. Cyclosporin H is used experimentally as an FPR1 antagonist, and no FPR1-selective drug is currently approved for therapeutic use. FPR1 receptor desensitization, β-arrestin recruitment and internalization are regulated by phosphorylation of carboxyl-terminal serine338/threonine339 (pS338/pT339-FPR1). This nomenclature refers to the human FPR1 receptor. For more information on FPR1 pharmacology please refer to the IUPHAR database. For further reading refer to:

Ye RD, Boulay F, Wang JM, Dahlgren C, Gerard C, Parmentier M, Serhan CN, Murphy PM. International Union of Basic and Clinical Pharmacology. LXXIII. Nomenclature for the formyl peptide receptor (FPR) family. Pharmacol Rev. 2009 Jun;61(2):119-61. doi: 10.1124/pr.109.001578. Epub 2009 Jun 4. PMID: 19498085; PMCID: PMC2745437.