Recombinant Human GALNT13 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 8906-GT

R&D Systems, part of Bio-Techne
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8906-GT-020
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Key Product Details

Source

HEK293

Accession #

Q8IUC8

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Polypeptide GalNAc Transferase 13/GALNT13 Proteins and Enzymes »

Product Specifications

Source

Human embryonic kidney cell, HEK293-derived human Polypeptide GalNac Transferase 13/GALNT13 protein
Ser29-Thr556, with a C-terminal 6-His tag

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

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

N-terminal Sequence Analysis

Ser29

Predicted Molecular Mass

61 kDa

SDS-PAGE

60-70 kDa, reducing conditions

Activity

Measured by its ability to transfer GalNAc from UDP-GalNAc to peptide EA2 from AnaSpec, Inc.
The specific activity is >600 pmol/min/μg, as measured under the described specifications.

Formulation, Preparation and Storage

8906-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 13/GALNT13

O-glycosylation is a ubiquitous post-translational modification present in secreted and membrane-bound proteins. Polypeptide N-acetylgalactosaminyltransferases (GALNTs) catalyze 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). GALNT13 is highly homologous to ubiquitously expressed GALNT1, but is restrictively expressed in the brain (7). In addition, GALNT13 is able to form trimeric Tn antigen, three consecutive GalNAc-Ser/Thr structures, on syndecans, which may further enhances cancer metastasis (7, 8). The enzymatic activity of recombinant human GALNT1 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. Zhang, Y. et al. (2003) J. Biol. Chem. 278:573.
  8. Matsumoto, Y. et al. (2013) J. Biol. Chem. 288:24264.
  9. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13

Alternate Names

Acetylgalactosaminyltransferase 13, GalNAc-T13, Pp-GaNTase 13

Entrez Gene IDs

114805 (Human)

Gene Symbol

GALNT13

UniProt

Q8IUC8

Additional Polypeptide GalNAc Transferase 13/GALNT13 Products

Product Documents for Recombinant Human GALNT13 Protein, CF

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Product Specific Notices for Recombinant Human GALNT13 Protein, CF

For research use only

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