Chst2 catalyzes the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N-linked glycans and within mucin-associated glycans that can ultimately serve as L-selectin ligands. L-selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Chst2 participates in biosynthesis of L-selectin ligand sialyl 6-sulfo Lewis X and in lymphocyte homing to Peyer patches. It has no activity toward O-linked sugars. Its substrate specificity may be influenced by its subcellular location. It sulfates GlcNAc residues at terminal, non-reducing ends of oligosaccharide chains.