Boletopsis grisea Lectin (BGL) is a recombinant 15 kDa lectin from the Boletopsis grisea mushroom that has been expressed in E. coli. BGL has two separately functioning ligand binding sites (1). Site 1 binds to O-glycans bearing the Tn antigen (GalNAc-α-Ser/Thr) or Thomsen-Friedenreich antigen (TF-antigen; Gal-β1,3-GalNAc-α-) and Site 2 binds N-glycans with terminal GlcNAc residues.
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