Anti-CD162 / PSGL-1 Monoclonal Antibody (Clone:TC2)-PE Conjugated

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.

Subcellular location:	Membrane
Post transnational modification:	Sulfation, in conjunction with the SLe(x)-containing glycan, is necessary for P- and L-selectin binding. High affinity P-selectin binding has a preferred requirement for the isomer sulfated on both Tyr-48 and Tyr-51, whereas L-selectin binding requires predominantly sulfation on Tyr-51 with sulfation on Tyr-48 playing only a minor role. These sulfations play an important role in L- and P-selectin-mediated neutrophil recruitment, and leukocyte rolling.
Tissue Specificity:	Expressed on neutrophils, monocytes and most lymphocytes.
BioGrid:	112304. 6 interactions.

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