General Notes
Mouse anti Human CD162 clone TC2, recognizes CD162 also known as P-Selectin glycoprotein ligand-1 (PSGL-1). It is a 120 kDa transmembrane protein that primarily exists as a homodimer on hematopoietic cells including myeloid, lymphoid, dendritic cells and some non-hematopoietic cells (Laszik et al. 1996). The most well know function of CD162, when activated, is its role in inflammation in that it slows down leucocytes on the surface of activated epithelium. This occurs when one of its ligands, P-, E- or L- selectin on activated platelets or activated endothelial cells bind to its N-terminal extracellular domain. Upon P-selectin binding, a very long molecule is essentially formed which extends from the activated endothelial cells and leukocyte surface layer, These can also effectively capture circulating myeloid cells. Before a ligand can bind to CD162, the receptor must be postranslationally modified with sialylated, fucosylated O-glycans as well as sulfation at the N-terminal tyrosines (Kappelmayer & Nagy 2017). Mutations which interrupt these post translational modifications prevent ligand binding and has been shown to result in patients suffering from infections of the mucosal membrane and skin (Maly et al. 1996). The TC2 clone has been used in flow cytometry experiments to examine the effects on CD162 expression levels on the surface of neutrophils upon treatment with histidine-rich glycoprotein which can regulate immunothrombosis and inflammation (Wake et al. 2016).