Human Polypeptide GalNAc Transferase 1/GALNT1 Antibody Summary
5% cross‑reactivity with recombinant human (rh) GALNT2 and rhGALNT3 is observed.
Accession # Q10472
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.
Polypeptide GalNac Transferase 1/GALNT1 in Human Liver. Polypeptide GalNac Transferase 1/GALNT was detected in immersion fixed paraffin-embedded sections of human liver using Sheep Anti-Human Polypeptide GalNac Transferase 1/GALNT1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7140) at 1 µg/mL overnight at 4 °C. Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using the Anti-Sheep HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS019) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm of hepatocytes. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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).
- Gerken, T.A. et al. (2011) J. Biol. Chem. 286:14493.
- Ten Hagen, K.G. et al. (2003) Glycobiology 13:1R.
- Hagen, F.K. et al. (1997) J. Biol. Chem. 272:13843.
- Gerken, T.A. et al. (2006) J. Biol. Chem. 281:32403.
- Pratt, M.R. et al. (2004) Chem. Biol. 11:1009.
- Miwa, H.E. et al. (2010) J. Biol. Chem. 285:1208.
- Wu, Z.L. et al. (2011) Glycobiology 21:727.
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