Human PSGL-1/CD162 (His & Fc Tag) recombinant protein

Human PSGL-1/CD162 (His & Fc Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

P-selectin glycoprotein ligand-1 (PSGL-1), also known as SELPLG or CD162, is the high affinitycounter-receptor for P-selectin on expressed on activated endothelial cells and platelets. PSGL-1 is a mucin-type glycoprotein, expressed on leukocytes and platelets as a homodimer of two disulfide-linked subunits of ~120 kD. As cell adhesion molecules, multiple studies have shown that PSGL-1/ P-selectin interaction is required for the normal recruitment of leukocytes during inflammatory reactions, and also participates in hemostatic responses. PSGL-1 protein requires two distinct posttranslational modifications for the Ca2+-dependent recognition by the lectin domain of P-selectin, that is tyrosine sulfation and specific O-linked glycosylation (sialic acid and fucose). PSGL-1 can also bind to other two members of the selectin family, E-selectin (endothelial) and L-selectin (leukocyte), but binds best to P-selectin.

P-selectin glycoprotein ligand 1

SELPL; CD162; SELP1; PSGL1; CLA; SELPLG; PSGL-1

Q14242

SELPLG

Human Cells

A DNA sequence encoding the extracellular domain (Met1-Val295) of human PSGL-1 precursor (AAC50061.1) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.

Human

The recombinant human PSGL-1/Fc is a disulfide-linked homodimer after removal of the signal peptide and the prppeptide. The reduced monomer consists of 526 amino acids and has a predicted molecular mass of 57.1 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh PSGL-1/Fc monomer is approximately 110-120 kDa due to glycosylation.

> 95 % as determined by SDS-PAGE