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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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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.
For broader research on PSGL-1/CD162 expression, selectin interactions and leukocyte trafficking, see our CD162 Antibody / P-Selectin Glycoprotein Ligand 1 Antibody page.
Optimal dilution of the recombinant CD162 antibody should be determined by the researcher.
Recombinant full-length human CD162 protein was used as the immunogen for the recombinant CD162 antibody.
Store the recombinant CD162 antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
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