P-Selectin/CD62P (human, recombinant)

P-selectin, also known as CD62P, is a glycoprotein and cell adhesion molecule that is encoded by the SELP gene in humans.{60879} It is a homodimer and is composed of an N-terminal calcium-dependent lectin domain that recognizes glycoproteins, an EGF-like domain, nine consensus repeats, a transmembrane domain, and an intracellular C-terminal tail. P-selectin is expressed in platelets, endothelial cells, and macrophages, is stored in ?-granules of platelets, and localizes to the plasma membrane upon platelet activation.{60888,60889,60879} It also exists as a soluble form that results from alternative splicing of SELP.{60879} P-selectin is involved in tethering and rolling of leukocytes during inflammation and tissue healing mediated by binding to P-selectin glycoprotein ligand-1 (PSGL-1), a mucin expressed on the surface of leukocytes.{60879,60890} In vivo, transgenic mice expressing human SELP exhibit neutrophil recruitment in a model of peritonitis induced by thioglycolate.{60888} Polymorphisms in SELP and serum levels of soluble P-selectin are associated with coronary artery disease.{60891} Cayman’s P-Selectin/CD62P (human, recombinant) protein can be used for cell-based assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of P-selectin/CD62P (amino acids 1-771) fused to human IgG1 Fc at its C-terminus, consists of 971 amino acids and has a calculated molecular weight of 107 kDa, and a predicted N-terminus of Trp42 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 130-150 kDa by SDS-PAGE under reducing conditions.