Recombinant Human GALNT2 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7507-GT

R&D Systems, part of Bio-Techne
Catalog #
Availability
Size / Price
Qty
7507-GT-020
Print Quote
Bulk Order
100% Guarantee

Key Product Details

Source

NS0

Accession #

Q10471

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Polypeptide GalNAc Transferase 2/GALNT2 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human GALNT2 protein
Lys52-Gln571, with N-terminal 6-His tag

Purity

>85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

His

Predicted Molecular Mass

60 kDa

SDS-PAGE

55-65 kDa, reducing conditions

Activity

Measured by its ability to transfer GalNAc from UDP-GalNAc to peptide EA2 from AnaSpec, Inc.
The specific activity is >350 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

7507-GT
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl and Brij-35.
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 2/GALNT2

O-glycosylation is a ubiquitous post-translational modification present in secreted and membrane-bound proteins. Polypeptide N-acetylgalactosaminyltransferases (GALNTs) catalyze the initial step of 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). Human GALNT2 is highly expressed in liver and skeletal muscle (7). Besides UDP-GalNAc, GALNT2 can also use UDP-Gal as a donor substrate (5). Along with GALNT1 and GALNT5, GALNT2 is classified as an early transferase that initiates glycosylation on mucin glycoproteins (6). The enzymatic activity of recombinant human GALNT2 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. White, T. et al. (1995) J. Biol. Chem. 270:24156.
  8. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2

Alternate Names

GalNAc-T2, Polypeptide GalNac Transferase 2, pp-GaNTase 2

Entrez Gene IDs

2590 (Human); 108148 (Mouse); 292090 (Rat)

Gene Symbol

GALNT2

UniProt

Q10471

Additional Polypeptide GalNAc Transferase 2/GALNT2 Products

Product Documents for Recombinant Human GALNT2 Protein, CF

Product Datasheets

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Download SDS

Product Specific Notices for Recombinant Human GALNT2 Protein, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

For research use only

Privacy and Cookie Policy
Site Map
© Copyright 2024 Bio-Techne. All Rights Reserved.