Recombinant Mouse PECAM-1 protein (His tag)

Specifications

Form

Lyophilized

General info

Function

Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (By similarity). Tyr-679 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes (By similarity). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (By similarity). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (By similarity). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (By similarity). Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes (By similarity). Modulates bradykinin receptor BDKRB2 activation (By similarity). Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (By similarity). Induces susceptibility to atherosclerosis (PubMed : 19048083).

Post-translational modifications

Phosphorylated on Ser and Tyr residues by src kinases after cellular activation (PubMed:16731527). Upon activation, phosphorylated on Ser-718 which probably initiates the dissociation of the membrane-interaction segment (residues 698-718) from the cell membrane allowing the sequential phosphorylation of Tyr-702 and Tyr-679 (By similarity). Constitutively phosphorylated on Ser-723 in resting platelets (By similarity). Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation (PubMed:16731527). In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation (By similarity).. Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts.