Recombinant Human GALNT14 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 9077-GT

R&D Systems, part of Bio-Techne
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9077-GT-050
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Key Product Details

Source

CHO

Accession #

Q96FL9

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Polypeptide GalNAc Transferase 14/GALNT14 Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Polypeptide GalNac Transferase 14/GALNT14 protein
Thr27-Ser552 with C-terminal 6-His tag

Purity

>90%, 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

Thr27

Predicted Molecular Mass

62 kDa

SDS-PAGE

56-64 kDa, reducing conditions

Activity

Measured by its ability to transfer GalNAc from UDP-GalNAc to peptide EA2 from AnaSpec, Inc.
The specific activity is >25 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

9077-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 14/GALNT14

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). GALNT14 transfers GalNAc to mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (7). GALNT14 is also a potential biomarker for breast cancer (8). The enzymatic activity of recombinant human GALNT14 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. Wang, H. et al. (2003) Biochem. Biophys. Res. Commun. 300:738.
  8. Wu, C, et al. (2010) BMC Cancer 10:123.
  9. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14

Alternate Names

GalNac-T14, GALNT15

Entrez Gene IDs

79623 (Human); 71685 (Mouse); 313878 (Rat)

Gene Symbol

GALNT14

UniProt

Q96FL9

Additional Polypeptide GalNAc Transferase 14/GALNT14 Products

Product Documents for Recombinant Human GALNT14 Protein, CF

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Product Specific Notices for Recombinant Human GALNT14 Protein, CF

For research use only

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