Recombinant Human GALNT1 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7140-GT

R&D Systems, part of Bio-Techne
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7140-GT-020
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Key Product Details

Source

NS0

Accession #

Q10472

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Polypeptide GalNAc Transferase 1/GALNT1 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human Polypeptide GalNac Transferase 1/GALNT1 protein
Gly41-Phe559, with an N-terminal 6-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Inconclusive results, intact N-terminus verified by anti-poly-His Western.

Predicted Molecular Mass

60 kDa

SDS-PAGE

60-65 kDa, reducing conditions

Activity

Measured by its ability to transfer GalNAc from UDP-GalNAc to peptide EA2 from AnaSpec, Inc.
The specific activity is >700 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

7140-GT
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

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

Product Documents for Recombinant Human GALNT1 Protein, CF

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Product Specific Notices for Recombinant Human GALNT1 Protein, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

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