CD31/PECAM-1 Protein, Cynomolgus (HEK293, His)

CD31/PECAM-1 protein, a pivotal cell adhesion molecule, is essential for leukocyte transendothelial migration (TEM) in most inflammatory conditions. The critical role of Tyr-679 in TEM is underscored by its requirement for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC), crucial for targeting the LBRC membrane around migrating leukocytes. The trans-homophilic interaction potentially contributes to endothelial cell-cell adhesion via cell junctions, while heterophilic interaction with CD177 plays a role in the transendothelial migration of neutrophils. Homophilic ligation of PECAM1 serves a dual purpose, preventing macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal, while promoting the macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to phagocytic cells. Notably, PECAM1 modulates bradykinin receptor BDKRB2 activation and regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells. Its interaction with various partners, including BDKRB2, GNAQ, PTPN11, FER, and CD177, further elucidates the intricate molecular mechanisms governing its diverse cellular functions, while its trans-homodimerization is crucial for effective cell-cell interaction. The interaction nuances, such as Ca(2+)-dependency and directness, add layers of complexity to the regulatory roles of CD31/PECAM-1.