GalNAc-T5, soluble fragment, Human Recombinant

Polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5) catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the hydroxyl group of serine and threonine residues, and was first cloned from rat. Twenty GalNAc-T genes have been identified in humans and most have been shown to represent active GalNAc-Ts. All isoforms are type II transmembrane proteins, with different but partly overlapping substrate preferences. The GalNAc-Ts control the initiation of mucin-type O-linked glycosylation and determine the location and density of O-glycans in a protein. Addition of GalNAc to an unglycosylated Ser/Thr residue creates the Tn antigen GalNAcα1-S/T, and subsequent addition of sialic acid by ST6GalNAc-I forms the cancer associated STn antigen. GalNAc-T5 expression pattern is highly regulated, and is most abundant in salivary glands. GalNAc-T5 has a preference for unglycosylated or monoglycosylated substrates.