O-glycosylation is a ubiquitous post-translational modification present in secreted and membrane-bound proteins. Polypeptide N-acetylgalactosaminyltransferases (GALNTs) calalyze the initial step for o-glycosylation by transferring GalNAc to Thr or Ser residues (GalNAc alpha1-O-Ser/Thr) in the Golgi compartment. Structurally, the GALNTs 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 (1, 2). Twenty distinct GALNT isoforms have been detected in humans. These isoforms display both unique and overlapping substrate specificities (3, 4, 5) with no known universal consensus glycosylation sequence. Glycosylation of mucins results from the successive, often hierarchical, action of several specific GALNTs (6). GALNT10 exhibits a single large preference for Ser/Thr-O-GalNAc at the +1 (C-terminal) position relative to the Ser or Thr acceptor site (7) and is able to glycosylate substrates of tri- and even tetraglycosylated peptides, which may complete mucin domain assembly; therefore it is classified as the late transferase (6). Human GALNT10 is found in the small intestine, stomach, pancreas, ovary, thyroid gland and spleen.
Source:Recombinant protein corresponding to aa71-603 from human GALNT10, fused to His-tag at C-terminal, NS0-derived.
Molecular Weight:~60-68kD
Endotoxin:<0.10EU/1ug (LAL method).
Storage and Stability::Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
