Human Polypeptide GalNAc Transferase 3/GALNT3 Antibody

Catalog # Availability Size / Price Qty
AF7174
AF7174-SP
Detection of Human and Mouse Polypeptide GalNac Transferase 3/GALNT3 by Western Blot.
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Product Details
Citations (3)
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Human Polypeptide GalNAc Transferase 3/GALNT3 Antibody Summary

Species Reactivity
Human
Specificity
Detects human Polypeptide GalNac Transferase 3/GALNT3 in direct ELISAs and Western blots. In direct ELISAs, less than 1% cross-reactivity with recombinant human (rh) GALNT1 and rhGALNT4 is observed.
Source
Polyclonal Sheep IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human Polypeptide GalNac Transferase 3/GALNT3
Gln38-Asp633
Accession # Q14435
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Applications

Recommended Concentration
Sample
Western Blot
0.5 µg/mL
See below
Immunocytochemistry
5-15 µg/mL
See below

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

Western Blot Detection of Human and Mouse Polypeptide GalNac Transferase 3/GALNT3 antibody by Western Blot. View Larger

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.

Immunocytochemistry Polypeptide GalNac Transferase 3/GALNT3 antibody in HeLa Human Cell Line by Immunocytochemistry (ICC). View Larger

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.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitution
Sterile PBS to a final concentration of 0.2 mg/mL.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 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).

References
  1. Gerken, T.A. et al. (2011) J. Biol. Chem. 286:14493.
  2. Ten Hagen, K.G. et al. (2003) Glycobiology 13:1R.
  3. Hagen, F.K. et al. (1997) J. Biol. Chem. 272:13843.
  4. Gerken, T.A. et al. (2006) J. Biol. Chem. 281:32403.
  5. Wandall, H.H. et al. (1997) J. Biol. Chem. 272:23503.
  6. Pratt, M.R. et al. (2004) Chem. Biol. 11:1009.
  7. Bennett, E.P. et al. (1996) J. Biol. Chem. 271:17006.
  8. Wu, Z.L. et al. (2011) Glycobiology 21:727.
Long Name
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Entrez Gene IDs
2591 (Human); 144251 (Mouse); 366061 (Rat)
Alternate Names
EC 2.4.1.41; GalNAc transferase 3; GalNAc-T3; GalNAc-T3DKFZp686C10199; GALNT3; HFTC; HFTCMGC61909; HHS; HHSPolypeptide GalNAc transferase 3; polypeptide GalNAc-transferase T3; polypeptide N-acetylgalactosaminyltransferase 3; pp-GaNTase 3; Protein-UDP acetylgalactosaminyltransferase 3; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3; UDP-N-acetyl-alpha-D-galactosamine:polypeptideN-acetylgalactosaminyltransferase 3 (GalNAc-T3)

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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.

3 Citations: Showing 1 - 3
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  1. 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
  2. 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
  3. 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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