Activated nucleotide sugar donor substrate for galactosyltransferases (GalTs); essential for the biosynthesis of N-glycans, O-glycans, glycolipids, and lactose; key substrate in the Leloir pathway and in glycoengineering of therapeutic antibodies (Fc galactosylation); also used in enzymatic synthesis of galactosylated glycoconjugates and in vitro glycosylation assays
Activated nucleotide sugar donor substrate for N-acetylgalactosaminyltransferases (GalNAc-Ts / ppGalNAc-Ts); initiates mucin-type O-linked glycosylation by transferring GalNAc to serine/threonine residues of proteins (Tn antigen formation); also involved in glycolipid biosynthesis, chondroitin sulfate chain elongation, and blood group A antigen synthesis; widely used in in vitro glycosylation assays and glycoengineering
Azido-modified analogue of UDP-GalNAc; serves as a substrate for N-acetylgalactosaminyltransferases (ppGalNAc-Ts) enabling metabolic and chemoenzymatic glycan labeling; the azidoacetyl handle permits bioorthogonal conjugation via copper-catalyzed azide–alkyne cycloaddition (CuAAC) and strain-promoted azide–alkyne cycloaddition (SPAAC); widely used in O-GalNAc glycoproteomics, mucin-type glycan imaging, and site-specific antibody–drug conjugate (ADC) construction
Activated nucleotide sugar donor substrate for N-acetylglucosaminyltransferases (GnTs / OGT); end product of the hexosamine biosynthetic pathway (HBP) and a key metabolic sensor linking nutrient status to glycosylation; essential for N-glycan branching (GnT-I through GnT-V), O-GlcNAc modification of nuclear and cytoplasmic proteins, chitin biosynthesis, and peptidoglycan assembly; widely used in in vitro glycosylation assays, glycoengineering, and metabolic studies
Azido-modified analogue of UDP-GlcNAc; serves as a substrate for O-GlcNAc transferase (OGT) and N-acetylglucosaminyltransferases enabling metabolic and chemoenzymatic glycan labeling; the azidoacetyl handle permits bioorthogonal conjugation via copper-catalyzed azide–alkyne cycloaddition (CuAAC) and strain-promoted azide–alkyne cycloaddition (SPAAC); can be epimerized to UDP-GalNAz by UDP-galactose-4-epimerase (GALE); widely used in O-GlcNAc proteomics, glycan imaging, and selective probing of intracellular O-GlcNAcylation
Activated nucleotide sugar donor substrate for glucosyltransferases; central metabolite in the Leloir pathway serving as precursor to UDP-Gal (via UDP-galactose-4-epimerase), UDP-GlcA (via UDP-glucose dehydrogenase), and glycogen (via glycogen synthase); essential for glycoprotein quality control (calnexin/calreticulin cycle), cellulose biosynthesis in plants, and trehalose synthesis; widely used in enzymatic glycosylation assays and metabolic studies