Thrombin Receptor (42 - 48) Agonist, human SFLLRNP
% Peak Area By HPLC ≥ 95%
Thrombin binds to its receptor's long N-terminal extracellular extension and cleaves the peptide bond between Arg-41 and Ser-42. The newly exposed N-terminal moiety starting from SFLLRNP acts as a tethered ligand to activate the receptor. It can also stimulate phosphoinositide turnover because the extent of phosphoinositide hydrolysis is directly proportional to the concentration of thrombin. The phenylalanine residue at position 2 is known to play a crucial role in the activation of the thrombin receptor in an intramolecular manner. On the other hand, agonist peptides incorporating the amino acid sequence (SFLLRNP) of the newly exposed N-terminal portion of the cleaved receptor cause receptor activation without requiring prior cleavage of the receptor by thrombin.
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