Recombinant Human GALNT4 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7528-GT

R&D Systems, part of Bio-Techne
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7528-GT-020
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Key Product Details

Source

NS0

Accession #

Q8N4A0

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Polypeptide GalNAc Transferase 4/GALNT4 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human Polypeptide GalNac Transferase 4/GALNT4 protein
Ala36-Lys578, with C-terminal 6-His tag

Purity

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

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

N-terminal Sequence Analysis

Ala36

Predicted Molecular Mass

64 kDa

SDS-PAGE

57-62 kDa, reducing conditions

Activity

Measured by its ability to transfer GalNAc from UDP-GalNAc to peptide EA2 from AnaSpec, Inc.
The specific activity is >200 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

7528-GT
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with dry ice or equivalent. 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, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: Polypeptide GalNAc Transferase 4/GALNT4

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). Human GALNT4 is widely expressed with particularly high expression in the immune system (7). The enzymatic specificity of GALNT4 depends on the selective binding between the C-terminal lectin domain and the existing O-GalNAc modified residues present within the substrate polypeptide (8). Along with GALNT3, GALNT4 is classified as an intermediate transferase that glycosylates mucin polypeptides that have been previously mono- or di-glycosylated by other transferases (6). The enzymatic activity of recombinant human GALNT4 was determined using a phosphatase-coupled assay (9).

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. (1998) J. Biol. Chem. 273:30472.
  8. Hassan, H. et al. (2000) J. Biol. Chem. 275:38197.
  9. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 4

Alternate Names

GALNACT4

Entrez Gene IDs

8693 (Human); 14426 (Mouse); 500826 (Rat)

Gene Symbol

GALNT4

UniProt

Q8N4A0 (Human)

Additional Polypeptide GalNAc Transferase 4/GALNT4 Products

Product Documents for Recombinant Human GALNT4 Protein, CF

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Product Specific Notices for Recombinant Human GALNT4 Protein, CF

For research use only

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