The N-formyl peptide receptor (FPR) family is comprised of three members, FPR, FPR like-1 (FPRL1, also designated lipoxin A4 receptor, FPRH1 and FPR2) and FPR like-2 (FPRL2), all of which are chemotactic G protein-coupled receptors that contain seven transmembrane domains. These receptors are found on the surface of phagocytic leukocytes, such as neutrophils and monocytes, and each family member contains specific residues, which are responsible for determining its ligand specificity. FPRL1 is a promiscuous receptor that binds to several ligands, including lipoxin A4, N-formyl-methionyl-leucyl-phenylalanine (fMLP), serum amyloid A (SAA), prion peptide and the 42 amino acid form of b-Amyloid. Upon activation, FPRL1 induces migration and calcium mobilization in human monocytes and neutrophils and is involved in inflammatory and host defense responses. FPRL1 may mediate inflammation in prion and Alzheimer’s diseases, which makes it a potential target for therapeutic agents.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of FPR2 and, to a lesser extent, other FPR family members of mouse and rat origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 208-280 mapping within an internal region of FPR2 of mouse origin
Tissue Specificity
epitope corresponding to amino acids 208-280 mapping within an internal region of FPR2 of mouse origin