Description
Product Characteristics: CD162 (P-selectin glycoprotein ligand-1, PSGL-1) is a sialomucin constitutively expressed as a disulfide-linked homodimer of two 120 kDa subunits on the surface of circulating leukocytes. CD162 serves as a ligand for P- E- and L-selectin, with the highest affinity for P-selectin. It is thus involved in leukocyte rolling at the endothelial surfaces, prerequisite for firm leukocyte adhesion and subsequent transendothelial migration. CD162 also mediates leukocyte-platelet adhesion and interleukocyte contacts. Whereas serving as an adhession molecule on mature leukocytes, CD162 is a potent negative regulator of human hematopoietic progenitors.
Target Information: This gene encodes a glycoprotein that functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans, for its high-affinity binding activity. Aberrant expression of this gene and polymorphisms in this gene are associated with defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Apr 2011]