Anti-glucosaminyl (N-acetyl) transferase 1 antibodies are used for the immunodetection of the protein encoded by the GCNT1 gene. In humans, the canonical protein has a reported length of 428 amino acid residues and a mass of 49.8 kDa. Its subcellular localization is in the Golgi. It is reported to be highly expressed in activated T-lymphocytes and myeloid cells. A member of the Glycosyltransferase 14 protein family, it is a reported glycosyltransferase that catalyzes the transfer of an N-acetylglucosamine (GlcNAc) moiety in beta1-6 linkage from UDP-GlcNAc onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan. Post-translational modifications have been described, including glycosylation. Other names for this target antigen include C2GNT-L, C2GNT1, C2GlcNAcT, G6NT, NACGT2, and C2GNT. Gene orthologs have been identified in the mouse, rat, bovine, frog, chimpanzee and chicken species.