Human Polypeptide GalNAc Transferase 1/GALNT1 Alexa Fluor® 488-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Polypeptide GalNAc Transferase 1/GALNT1

O-glycosylation is a ubiquitous post-translational modification of secreted and membrane-bound proteins. Polypeptide N‑acetylgalactosaminyl­transferases (GALNTs) calalyze the initial step for o‑glycosylation: 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. Most of the isoforms display both unique and overlapping substrate specificities (3, 4) with no universal consensus glycosylation sequence. Glycosylation of mucins results from successive, often hierarchical, action of several specific GALNTs (5). GALNT1, in particular, is involved in the glycosylation of proteins essential for bone formation such as osteopontin and bone sialoprotein (6). Using a peptide library screening approach, GALNT1 was classified as an early transferase that has a preference for nonglycosylated or monoglycosylated substrates (5). The enzymatic activity of recombinant human GALNT1 was determined using a phosphatase-coupled assay (7).

Product Datasheets

Related Research Areas

• Glycobiology-related Enzymes
• Search Glycobiology-related Enzymes