Mouse PSGL-1/CD162 (Fc Tag) recombinant protein

Mouse PSGL-1/CD162 (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

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

Q62170

Selplg; Selp1; Selpl

Human Cells

A DNA sequence encoding the extracellular domain of mouse SELPLG (Q62170) (Met 1-Cys 307) was fused with the Fc region of human IgG1 at the C-terminus.

Mouse

The secreted recombinant mouse SELPLG/Fc is a disulfide-linked homodimer. The reduced monomer comprises 531 amino acids and has a calculated molecular mass of 57.4 kDa. As a result of glycosylation, the apparent molecular mass of rmSELPLG/Fc monomer is approximately 82 kDa in SDS-PAGE under reducing conditions.

> 85 % as determined by SDS-PAGE