Anti-PECAM-1 (CD31) Antibody, clone TLD-3A12 clone TLD-3A12, from mouse

Platelet endothelial cell adhesion molecule (UniProt: Q3SWT0; PECAM-1, CD31) is encoded by the Pecam1 (also known as Pecam) gene (Gene ID: 29583) in rat.PECAM-1 is a single-pass type I membrane protein that contains 6 Ig-like C2-type (immunoglobulin-like) domains. PECAM1 is differentially glycosylated involving both N-linked and O-linked glycosylation sites. It is a cell adhesion molecule that is required for leukocyte trans-endothelial migration (TEM) under most inflammatory conditions. PECAM1 plays a vital role in signaling processes involved in angiogenesis, platelet function, thrombosis, mechanosensing of endothelial cell response to fluid shear stress, and regulation of multiple stages of leukocyte migration through venular walls. PECAM1 is expressed on platelets and leukocytes and is primarily concentrated at the borders between endothelial cells. PECAM1 prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes. During apoptosis, the inside-out signaling of PECAM1 is disabled that allows the apoptotic cell to accept phagocyte interaction. PECAM1 is phosphorylated on serine and tyrosine residues following cellular activation. In endothelial cells Fyn is shown to mediate mechanical-force induced tyrosine phosphorylation. In response to Fc epsilon RI (FCER1 activation), PECAM1 is phosphorylated on tyrosine residues by FER and FES.