Human Polypeptide GalNAc Transferase 3/GALNT3 Antibody
Human Polypeptide GalNAc Transferase 3/GALNT3 Antibody Summary
Gln38-Asp633
Accession # Q14435
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.
Scientific Data
Detection of Human and Mouse Polypeptide GalNac Transferase 3/GALNT3 by Western Blot. Western blot shows lysates of COLO 205 human colorectal adenocarcinoma cell line, MCF-7 human breast cancer cell line, and mouse testis tissue. PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human Polypeptide GalNac Transferase 3/GALNT3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7174) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Polypeptide GalNac Transferase 3/GALNT3 at approximately 75 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Polypeptide GalNac Transferase 3/GALNT3 in HeLa Human Cell Line. Polypeptide GalNac Transferase 3/GALNT3 was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line using Sheep Anti-Human Polypeptide GalNac Transferase 3/GALNT3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7174) at 15 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (red; Catalog # NL010) and counterstained with DAPI (blue). Specific staining was localized to Golgi granules. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
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 3/GALNT3
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 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). Expression of GALNT3 appears to be highly regulated and mainly found in pancreas and testis (7). Using a peptide library screening approach, GALNT3 was classified as an intermediate transferase that increases the density of O-linked glycans within the mucin domain following glycosylation with early transferases (5). The enzymatic activity of recombinant human GALNT3 was determined using a phosphatase‑coupled assay (8).
- 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.
- Wandall, H.H. et al. (1997) J. Biol. Chem. 272:23503.
- Pratt, M.R. et al. (2004) Chem. Biol. 11:1009.
- Bennett, E.P. et al. (1996) J. Biol. Chem. 271:17006.
- Wu, Z.L. et al. (2011) Glycobiology 21:727.
Product Datasheets
Citations for Human Polypeptide GalNAc Transferase 3/GALNT3 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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O-GalNAc glycosylation determines intracellular trafficking of APP and A? production
Authors: Tachida, Y;Iijima, J;Takahashi, K;Suzuki, H;Kizuka, Y;Yamaguchi, Y;Tanaka, K;Nakano, M;Takakura, D;Kawasaki, N;Saito, Y;Manya, H;Endo, T;Kitazume, S;
The Journal of biological chemistry
Species: Human
Sample Types: Peptides
Applications: Mass Spectrometry -
Argonaute binding within 3'-untranslated regions poorly predicts gene repression
Authors: Y Chu, A Kilikevici, J Liu, KC Johnson, S Yokota, DR Corey
Nucleic Acids Res., 2020-07-27;0(0):.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot -
Analysis of the glyco-code in pancreatic ductal adenocarcinoma identifies glycan-mediated immune regulatory circuits
Authors: Rodriguez E, Boelaars K, Brown K et al.
Communications biology
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