Polypeptide GalNac Transferase 3/GALNT3 Antibody

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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 ...read more
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 ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications WB, ICC/IF
Clonality
Polyclonal
Host
Sheep
Conjugate
Unconjugated
Concentration
LYOPH

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Catalog# & Formulation Size Price

Polypeptide GalNac Transferase 3/GALNT3 Antibody Summary

Immunogen
Mouse myeloma cell line NS0-derived recombinant human Polypeptide GalNac Transferase 3/GALNT3
Gln38-Asp633
Accession # Q14435
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
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Sheep
Gene
GALNT3
Purity
Immunogen affinity purified
Innovator's Reward
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Applications/Dilutions

Dilutions
  • Western Blot 0.5 ug/mL
  • Immunocytochemistry 5-15 ug/mL

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Concentration
LYOPH
Purity
Immunogen affinity purified
Reconstitution Instructions
Sterile PBS to a final concentration of 0.2 mg/mL.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Polypeptide GalNac Transferase 3/GALNT3 Antibody

  • 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)

Background

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).
  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.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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Bioinformatics

Gene Symbol GALNT3
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