Human Polypeptide GalNAc Transferase 3/GALNT3 Alexa Fluor™ Plus 647-conjugated Antibody

R&D Systems, part of Bio-Techne | Catalog # AF7174AFP647

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AF7174AFP647-100UG
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Key Product Details

Species Reactivity

Human

Applications

Western Blot, Immunocytochemistry

Label

Alexa Fluor Plus 647 (Excitation = 658 nm, Emission = 675 nm)

Antibody Source

Polyclonal Sheep IgG

View all Polypeptide GalNAc Transferase 3/GALNT3 Antibodies »

Product Specifications

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.

Clonality

Polyclonal

Host

Sheep

Isotype

IgG

Applications

Application
Recommended Usage

Immunocytochemistry

Optimal dilution of this antibody should be experimentally determined.

Western Blot

Optimal dilution of this antibody should be experimentally determined.

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 alpha1-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

Alternate Names

GalNAc-T3, HFTC, HHS, pp-GaNTase 3

Entrez Gene IDs

2591 (Human); 144251 (Mouse); 366061 (Rat)

Gene Symbol

GALNT3

UniProt

Q14435 (Human)

Additional Polypeptide GalNAc Transferase 3/GALNT3 Products

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Product Specific Notices


This product is provided under an intellectual property license from Life Technologies Corporation. The transfer of this product is conditioned on the buyer using the purchased product solely in research conducted by the buyer, excluding contract research or any fee for service research, and the buyer must not (1) use this product or its components for (a) diagnostic, therapeutic or prophylactic purposes; (b) testing, analysis or screening services, or information in return for compensation on a per-test basis; or (c) manufacturing or quality assurance or quality control, and/or (2) sell or transfer this product or its components for resale, whether or not resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.

For research use only

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