Recombinant Human GALNT10 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7575-GT

R&D Systems, part of Bio-Techne
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7575-GT-020
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Key Product Details

Source

NS0

Accession #

Q86SR1

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Polypeptide GalNAc Transferase 10/GALNT10 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human Polypeptide GalNac Transferase 10/GALNT10 protein
Leu71-Asn603, with a C-terminal 6-His tag

Purity

>80%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

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

N-terminal Sequence Analysis

Leu71

Predicted Molecular Mass

62 kDa

SDS-PAGE

60-68 kDa, reducing conditions

Activity

Measured by its ability to transfer GalNAc from UDP-GalNAc to peptide MUC5AC-3/13 from AnaSpec, Inc.
The specific activity is >180 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

7575-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 10/GALNT10

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). GALNT10 exhibits a single large preference for Ser/Thr‑O‑GalNAc at the +1 (C‑terminal) position relative to the Ser or Thr acceptor site (7) and is able to glycosylate substrates of tri‑ and even tetraglycosylated peptides, which may complete mucin domain assembly; therefore it is classified as the late transferase (6). Human GALNT10 is found in the small intestine, stomach, pancreas, ovary, thyroid gland and spleen (8). The enzymatic activity of recombinant human GALNT10 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. Perrine, C.L. et al. (2009) J. Biol. Chem. 284:20387.
  8. Cheng, L. et al. (2002) FEBS Lett. 531:115.
  9. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10

Alternate Names

GalNAc-T10, PPGALNACT10, PPGANTASE10

Entrez Gene IDs

55568 (Human); 171212 (Mouse); 170501 (Rat)

Gene Symbol

GALNT10

UniProt

Q86SR1 (Human)

Additional Polypeptide GalNAc Transferase 10/GALNT10 Products

Product Documents for Recombinant Human GALNT10 Protein, CF

Product Datasheets

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Product Specific Notices for Recombinant Human GALNT10 Protein, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

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