Recombinant Human GALNT11 Protein, CF

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

O-glycosylation is a ubiquitous post-translational modification present in secreted and membrane-bound proteins. Polypeptide N-acetylgalactosaminyltransferases (GALNTs) catalyze the initial step for O-glycosylation by transferring GalNAc to Thr or Ser residues (GalNAc alpha 1-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). GALNT11 catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (7); therefore it should be classified as an early transferase that has a preference for nonglycosylated or monoglycosylated substrates. GALNT11 is highly expressed in kidney and at intermediate level in brain, heart and skeletal muscle (7). GALNT11 is crucial to determine left-right asymmetry by O-glycosylating human Notch receptor 1 (8). The enzymatic activity of recombinant human GALNT11 was determined using a phosphatase-coupled assay (9).

Array 8905-GT

• GALNT11 Antibodies
• GALNT11 Protein
• GALNT11 Proteins and Enzyme