Recombinant Human P-Selectin/CD62P Fc Chimera Protein, CF

Human P-Selectin (GMP-140, LECAM-3, PADGEM, CD62P), a member of the Selectin family, is a cell surface glycoprotein expressed by activated platelets and endothelial cells. P-Selectin is translocated to the cell surface within minutes, from alpha granules of platelets or Weibel-Palade bodies of endothelial cells, following stimulation with thrombin, histamine, PMA or peroxides. P-Selectin binds to a 106 kDa protein present on myeloid cells, neutrophils, monocytes and lymphocytes, termed PSGL-1 (P-Selectin glycoprotein ligand-1).

P-Selectin plays a role in the adhesion of leukocytes and neutrophils to the endothelium. Acting in cooperation with L-Selectin, P-Selectin mediates the initial interaction of circulating leukocytes with endothelial cells that produces a characteristic ‘rolling’ of the leukocytes on the endothelium. This initial interaction is followed by a stronger interaction involving E-Selectin, and later ICAM-1 and VCAM-1, that leads eventually to extravasation of the white blood cell through the blood vessel wall into the extracellular matrix tissue.

Human P-Selectin cDNA encodes an 830 amino acid (aa) residue type I transmembrane protein with a 41 aa signal peptide, a 730 aa extracellular domain, a transmembrane domain and a short (35 aa) cytoplasmic domain. The extracellular domain has an NH₂-terminal C-type lectin domain and an EGF-like domain followed by a series of complement factor A repeat homology domains. The extracellular domains of human and mouse P-Selectin share approximately 73% sequence homology.