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Formalin-fixed, paraffin-embedded human tonsil stained with CD162 Recombinant Rabbit Monoclonal Antibody (PSGL1/8192R). HIER: Tris/EDTA, pH9.0, 45min. 2: HRP-polymer, 30min. DAB, 5min.
CD162 glycoprotein 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. �
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