Polypeptide N-acetylgalactosaminyltransferase 5 (UniProt: Q7Z7M9; also known as EC:2.4.1.41, Polypeptide GalNAc transferase 5, GalNAc-T5, pp-GaNTase 5, Protein-UDP acetylgalactosaminyltransferase 5, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5) is encoded by the GALNT5 gene (Gene ID: 11227) in human. Complex carbohydrates synthesis in mammals involves over 200 distinct glycosyltransferases that differ in their cellular expression and their glycosylation capacity. A majority of them are localized in the endoplasmic reticulum or Golgi and their specific subcellular localization is believed to be distributed in the secretory pathway according to their sequential role in the glycosylation process. GalNAc-T5 is a single-pass type II membrane glycoprotein with a cytoplasmic domain (aa 1-12), a transmembrane domain (aa 13-35), and a lumenal domain (aa 36-940). It 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. It displays activity toward EA2 peptide substrates but has a weak activity toward Muc2 or Muc1b substrates. GalNAc-T5 has two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif) that is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif) that is involved in catalytic reaction and UDP-Gal binding. It also contains a ricin B-type lectin domain (aa 804-935) that binds to GalNAc and contributes to the glycopeptide specificity. Strong expression of GalNAc-T5 has been reported in normal gastric epithelium and in gastric cancer cells. However, its expression in normal gastric tissues is limited to a perinuclear Golgi-like localization and it is expressed throughout the cytoplasm of gastric cancer cells. (Ref.: Steentoft, C., et al. (2019). Glycobiology. 29(9); 645-656; Campos, D., et al. (2015). Mol. Cell. Proteomics. 14(6); 1616-1629).

Clone 5F11 is a mouse monoclonal antibody that detects GalNAc transferase 5 (GalNAc-T5).

His-tagged, full-length recombinant human GalNAc-T5 expressed in Sf9 insect cells.

Quality Control Testing

Evaluated by Immunohistochemistry in human colon tissue sections.

Immunohistochemistry Analysis: A 1:50 dilution of this antibody detected GalNAc-T5 in human colon tissue sections.

Tested Applications

Immunocytochemistry Analysis: A representative lot detected GalNAc-T5 in Immunocytochemistry application (Campos, D., et al. (2015). Mol Cell Proteomics.14(6);1616-29; Norden, R., et al. (2015). J Biol Chem. 290(8); 5078-5091; Steentoft, C., et al. (2019). Glycobiology. 29(9); 645-656).

Immunofluorescence Analysis: A representative lot detected GalNAc-T5 in Immunofluorescence application (Campos, D., et al. (2015). Mol Cell Proteomics. 14(6); 1616-29; Norden, R., et al. (2015). J Biol Chem. 290(8); 5078-5091).

Immunohistochemistry Application : A representative lot detected GalNAc-T5 in Immunohistochemistry application (Campos, D., et al. (2015). Mol Cell Proteomics. 14(6); 1616-29.

Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user

Anti-GalNAc-T5, clone 5F11, Cat. No. MABS2302, is a mouse monoclonal antibody that detects GalNAc-T5 and is tested for use in Immunocytochemistry, Immunofluorescence, and Immunohistochemistry.

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Recommended storage: +2°C to +8°C.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.