Anti-PECAM-1, clone C31.7

Prediluted in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide, *For IHC use only*. PECAM-1, or platelet endothelial cell adhesion molecule-1, also called CD31, is made up of six extracellular immunoglobulin-like domains, a single transmembrane domain, and a cytoplasmic domain containing serine and tyrosine residues that when phosphorylated, activate the molecules signaling function. It is expressed on platelets, monocytes, neutrophils, bone marrow macrophage and dendritic cells precursors, and at the intracellular junction of endothelial cells. PECAM-1, on the endothelial lining of blood vessels, helps maintain the vascular barrier. In response to inflammatory mediators, the endothelial pull away from each other allowing fluid, inflammatory cells and proteins into the extravascular space. The inflammatory response fades as adhesion of neighboring cells increase. PECAM-1 also plays an important role in angiogenesis, promoting endothelial cell motility, junctional development and capillary morphogenesis. 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]