Recombinant human GalNAc Transferase 1/GALNT1 protein

GALNT1, also known as polypeptide N-acetylgalactosaminyltransferase 1, is a member of the GalNAc-T family of enzymes. It utilizes UDP-GalNAc as the nucleotide donor substrate to modify serine or threonine residues of proteins trafficking through the secretory pathway. Structurally, GalNAc-Ts consist of an N-terminal catalytic domain tethered by a short linker to a C-terminal ricin-like lectin domain containing three potential carbohydrate-binding sites. Also, this protein is involved in the glycosylation of proteins essential for bone formation such as osteopontin and bone sialoprotein. Recombinant human GALNT1, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques.