Recombinant human PSGL-1/CD162 protein

PSGL-1, also known CD162 or SELPLG, is a mucin-type glycoprotein that functions as a high affinity counter-receptor for the cell adhesion molecules P-, Eand L- selectin expressed on myeloid cells and stimulated T lymphocytes. This protein plays a key role in leukocyte adhesion. As such, it plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. PSGL-1 binds chmokines such as CCL19, CCL21, and CCL27, promoting chemotaxis of hematopoietic stem cells and plasma cells to the bone marrow and T cell homing to lymphoid organs. 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. Recombinant human PSGL-1, fused to hIgG-His-tag at C-terminus, was expressed in HEK293 cell and purified by using conventional chromatography techniques.