PSGL-1/CD162 Proteins, Antibodies, cDNA Clones Research Reagents

SELPLG (Selectin P Ligand) is a protein coding gene located on human chromosome 12q24.11. SELPLG is also known as CLA, CD162, PSGL1 and PSGL-1. The human SELPLG gene encodes a 43201 Da protein containing 412 amino acids. The SELPLG protein is broadly expressed in spleen, lymph node and other tissues. Among its related pathways are amb2 Integrin signaling and Cell surface interactions at the vascular wall. SELPLG is related to signaling receptor binding. SELPLG is associated with some diseases, including Human Granulocytic Anaplasmosis and Ehrlichiosis.

PSGL-1/CD162 Protein (5)

    PSGL-1/CD162 Antibody (21)

      PSGL-1/CD162 cDNA Clone (26)


      PSGL-1/CD162 Lysate (5)

        PSGL-1/CD162 Background

        P-selectin glycoprotein ligand-1 (PSGL-1), also known as SELPLG or CD162, is the high affinity ounter-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 ~12 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.

        PSGL-1/CD162 References

        • 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.

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