Anti-PECAM-1, clone C31.7

1 mg/ml in sterile PBS, BSA free, sodium azide free. 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: Induces susceptibility to atherosclerosis. Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. 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. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC). [The UniProt Consortium]