Recombinant Human GALNT12 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 9074-GT

R&D Systems, part of Bio-Techne
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9074-GT-010
9074-GT-050
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Key Product Details

Source

CHO

Accession #

Q8IXK2

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Polypeptide GalNAc Transferase 12/GALNT12 Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Polypeptide GalNac Transferase 12/GALNT12 protein
Arg38-Leu581 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

Arg38

Predicted Molecular Mass

64 kDa

SDS-PAGE

58-67 kDa, reducing conditions

Activity

Measured by its ability to transfer GalNAc from UDP-GalNAc to peptide EA2 from AnaSpec, Inc.
The specific activity is >90 pmol/min/μg, as measured under the described conditions. See Activity Protocol on www.RnDSystems.com.

Formulation, Preparation and Storage

9074-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 12/GALNT12

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). GALNT12 has activity toward non-glycosylated mucin peptides such as Muc5AC, Muc1a and EA2, and displays enzymatic activity toward mono-GalNAc-glycosylated Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs (7). The enzymatic activity of recombinant human GALNT12 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. Guo, J.M. et al. (2002) FEBS Lett. 524:211.
  8. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12

Alternate Names

CRCS1, GalNAc-T12, Pp-GaNTase 12

Entrez Gene IDs

79695 (Human); 230145 (Mouse); 313233 (Rat)

Gene Symbol

GALNT12

UniProt

Q8IXK2

Additional Polypeptide GalNAc Transferase 12/GALNT12 Products

Product Documents for Recombinant Human GALNT12 Protein, CF

Product Datasheets

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Product Specific Notices for Recombinant Human GALNT12 Protein, CF

For research use only

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