Recombinant Human GALNT11 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 8905-GT

R&D Systems, part of Bio-Techne
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8905-GT-020
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Key Product Details

Source

CHO

Accession #

Q8NCW6

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Polypeptide GalNAc Transferase 11/GALNT11 Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Polypeptide GalNac Transferase 11/GALNT11 protein
Phe30-Gly608, with 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

Phe30

Predicted Molecular Mass

66 kDa

SDS-PAGE

58-68 kDa, reducing conditions

Activity

Measured by its ability to transfer GalNAc from UDP-GalNAc to peptide EA2 from AnaSpec, Inc.
The specific activity is >75 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

8905-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 11/GALNT11

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). GALNT11 catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (7); therefore it should be classified as an early transferase that has a preference for nonglycosylated or monoglycosylated substrates. GALNT11 is highly expressed in kidney and at intermediate level in brain, heart and skeletal muscle (7). GALNT11 is crucial to determine left-right asymmetry by O-glycosylating human Notch receptor 1 (8). The enzymatic activity of recombinant human GALNT11 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. Schwientek T. et al. (2002) J. Biol. Chem. 277:22623.
  8. Boskovski M.T. et al. (2013) Nature 504:456
  9. Wu, Z. L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11

Alternate Names

GalNAc-T11, Pp-GaNTase 11

Entrez Gene IDs

63917 (Human); 231050 (Mouse); 311952 (Rat)

Gene Symbol

GALNT11

UniProt

Q8NCW6

Additional Polypeptide GalNAc Transferase 11/GALNT11 Products

Product Documents for Recombinant Human GALNT11 Protein, CF

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Product Specific Notices for Recombinant Human GALNT11 Protein, CF

For research use only

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