Human P-selectin glycoprotein ligand 1 (SELPLG, also named as CD162) gene encodes a glycoprotein that 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, CD162 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. Alternate splicing results in multiple transcript variants.

Full-length extracellular domain of human CD162 cDNA (18 – 320 aa, Isoform-II, derived from BC029782) was constructed with codon optimization and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal. This protein is expressed in E.coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.

1. May be used for in vitro non-glycosylated CD162 protein mediated P-selectin related tumor metastasis regulation study with this protein as either coating matrix protein or soluble factor.

2. May be used as CD162 protein-protein interaction assay.

3. As enzymatic substrate for various proteases.

4. As antigen for specific antibody production.