Anti-Hu CD62P Purified SELP Monoclonal Antibody

CD62P (P-selectin) is an adhesion glycoprotein that is expressed on platelets and endothelial cells upon their activation. Interaction between CD62P and its mucin-like ligand PSGL-1 (P-selectin glycoprotein ligand-1) expressed on the microvilli of most leukocytes supports leukocyte rolling along postkapillary venules at the earliest time of inflammation. Both CD62P and PSGL-1 are extended glycoproteins that form homodimers. CD62P dimerization is probably mediated through interactions of the transmembrane domains and stabilizes leukocyte tethering and rolling, probably by increasing rebinding within a bond cluster.

Human platelets. The antibody AK4 recognizes an extracellular epitope of CD62P (P-selectin), a 140 kD single chain type I transmembrane glycoprotein present in secretory alpha-granules in platelets, in Weibel-Palade bodies in endothelial cells and in megakaryocytes; it is relocated to the plasma membrane upon activation.

Stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Upon cell activation by agonists, P-selectin is transported rapidly to the cell surface.

Ca (2+) -dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG.