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

CD162,CLA,PSGL-1,PSGL1

Catalog Number P10490-H03H
Organism Species Human
Host Human Cells
Synonyms CD162,CLA,PSGL-1,PSGL1
Molecular Weight 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.
predicted N Leu 18
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction 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.
Bio-activity
Research Area Immunology |Innate Immunity |Granulocyte Markers
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background 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.
Reference

1. Sako, D. et al., 1993, Cell. 75: 1179-1186.

2. Wilkins, P. P. et al., 1995, J. Biol. Chem. 270: 22677-22680.

3. Frenette, P. S. et al., 2000, J. Exp. Med. 191: 1413-1422.

4. Vandendries, E.R .et al., 2004, Thromb. Haemost. 92: 459-466..

5. Pouyani, T. et al., 1995, Cell. 83: 333-343.