Human Polypeptide GalNAc Transferase 1/GALNT1 Alexa Fluor™ Plus 647-conjugated Antibody

R&D Systems, part of Bio-Techne | Catalog # AF7140AFP647

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AF7140AFP647-100UG
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Key Product Details

Species Reactivity

Human

Applications

Immunohistochemistry, Western Blot

Label

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

Antibody Source

Polyclonal Sheep IgG

View all Polypeptide GalNAc Transferase 1/GALNT1 Antibodies »

Product Specifications

Immunogen

Mouse myeloma cell line NS0-derived recombinant human Polypeptide GalNac Transferase 1/GALNT1

Specificity

Detects human Polypeptide GalNac Transferase 1/GALNT1 in direct ELISAs and Western blots. In direct ELISAs, less than

Clonality

Polyclonal

Host

Sheep

Isotype

IgG

Applications

Application
Recommended Usage

Immunohistochemistry

Optimal dilution of this antibody should be experimentally determined.

Western Blot

Optimal dilution of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Formulation

Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied

Background: Polypeptide GalNAc Transferase 1/GALNT1

O-glycosylation is a ubiquitous post-translational modification of secreted and membrane-bound proteins. Polypeptide N‑acetylgalactosaminyl­transferases (GALNTs) calalyze the initial step for o‑glycosylation: 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. Most of the isoforms display both unique and overlapping substrate specificities (3, 4) with no universal consensus glycosylation sequence. Glycosylation of mucins results from successive, often hierarchical, action of several specific GALNTs (5). GALNT1, in particular, is involved in the glycosylation of proteins essential for bone formation such as osteopontin and bone sialoprotein (6). Using a peptide library screening approach, GALNT1 was classified as an early transferase that has a preference for nonglycosylated or monoglycosylated substrates (5). The enzymatic activity of recombinant human GALNT1 was determined using a phosphatase-coupled assay (7).

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. Pratt, M.R. et al. (2004) Chem. Biol. 11:1009.
  6. Miwa, H.E. et al. (2010) J. Biol. Chem. 285:1208.
  7. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1

Alternate Names

GALNAC-T1, pp-GaNTase 1

Entrez Gene IDs

2589 (Human); 14423 (Mouse); 79214 (Rat)

Gene Symbol

GALNT1

UniProt

Q10472

Additional Polypeptide GalNAc Transferase 1/GALNT1 Products

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Certificate of Analysis

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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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