The mouse monoclonal antibody HI62P 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.
Selectin P,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.,P-selectin, GMP140, SELP, PADGEM, GRMP, LECAM3, PSEL