The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
FPR1 posseses two potential N-glycosylation sites in the N-terminus (Asn4 and Asn10) and one potential N-glycosylation site in the second extracellular loop (Asn179).
ab90418 lacks the N-glycosylation sites at Asn4 and Asn10. It is less active in terms of high-affinity agonist binding and agonist-stimulated [35S]GTPγS binding.
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Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Guanine nucleotide-binding protein G(i) subunit alpha-2
Lipoxin A4 receptor
N-formyl peptide receptor
N-formylpeptide chemoattractant receptor
FMLP (Formyl peptide receptor 1), a Chemoattractant Receptor, mediates chemotaxis, degranulation, and superoxide production, as part of the inflammatory response. Bacterial N-formylmethionyl peptides and Annexin A1, specific ligands for FMLP, attract polymorphonuclear neutrophils to sites of infection. FMLP receptors promote the phosphorylation and downregulation of CCR5, which has been shown to inhibit HIV infection. Therefore, ligands for an FMLP receptor may be able to inhibit HIV infection. FMLP has been reported in blood monocytes, neutrophils, and phagocytes, as well as in liver, astrocytes, and microglia. ESTs have been isolated from B-cell/lung/testis, blood, brain, eye, heart, liver/spleen, kidney, lung, pancreas, placenta, spleen, and uterus libraries.
The G protein family of signal transducers includes 5 heterotrimers, which are most clearly distinguished by their different alpha chains; they have virtually identical beta chains and similar gamma chains. G protein alpha inhibitor chain 2 is a subunit of the G(i) G protein, whose role is in inhibiting adenylate cyclase activity in response to bound GTP. The G proteins possess GTPase activity and are components of a complex membrane signaling system that includes membrane bound receptors. The system exists to modulate extracellular signals as they are transmitted into the cell.
Cell membrane; Multi-pass membrane protein.
has not yet been referenced specifically in any publications.