Anti-CD31 / PECAM-1 Monoclonal Antibody (Clone:MEM-05)

CD31 (platelet endothelial cell adhesion molecule-1, PECAM-1) is an inhibitory coreceptor involved in regulation of T cell and B cell signaling by a dual immunoreceptor tyrosine-based inhibitory motif (ITIM) that upon associated kinases-mediated phosphorylation provide docking sites for protein-tyrosine phosphatases. CD31 is expressed ubiquitously within the vascular compartment and is located mainly at junctions between adjacent cells. N-terminal Ig-like domain of CD31 is responsible for its homophilic binding, which plays an important role in cell-cell interactions. CD31 is a multifunctional molecule with diverse roles in modulation of integrin-mediated cell adhesion, transendothelial migration, angiogenesis, apoptosis, negative regulation of immunoreceptor signaling, autoimmunity, macrophage phagocytosis, IgE-mediated anaphylaxis and thrombosis. It is one of key regulatory molecules in vascular system. Protein function: Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (PubMed:19342684, PubMed:17580308). Tyr-690 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 (PubMed:19342684). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (PubMed:27958302). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (PubMed:17580308). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (PubMed:12110892). 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 (PubMed:12110892). Modulates bradykinin receptor BDKRB2 activation (PubMed:18672896). Regulates bradykinin- and hyperosmotic shock- induced ERK1/2 activation in endothelial cells (PubMed:18672896). Induces susceptibility to atherosclerosis. [The UniProt Consortium]