Background:PSGL-1
PSGL-1 (P-Selectin Glycoprotein Ligand 1) is type I transmembrane receptor found on the surface of neutrophils, monocytes, and most lymphocytes. It is expressed as a dimeric mucin-like glycoprotein that is N-glycosylated and contains both sialylated and fucosylated O-linked oligosaccharides. PSGL-1 binds to P-, E- and L-Selectins. The calcium-dependent high affinity interaction with P-, E-, and L-Selectin mediates the tethering and rolling of neutrophils, monocytes, and/or lymphocytes on endothelial cells.
原厂资料:
Specificity:Detects human PSGL‑1/CD162. Recognizes sLex-bearing core 2 O‑glycan stuctures. It does not recognize sLex on an extended core 1 O‑glycan. The sLex-bearing, core 2 O‑glycan structure decorates the P-Selectin ligand PSGL-1, and the presence of this glycan structure is required for high affinity P-Selectin binding (1). This antibody stains human and canine leukocytes but does not recognize monkey, mouse, rabbit, porcine, feline or bovine leukocytes.