Recombinant Human GALNT7 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7748-GT

R&D Systems, part of Bio-Techne
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7748-GT-020
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Key Product Details

Source

NS0

Accession #

Q86SF2

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Polypeptide GalNAc Transferase 7/GALNT7 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human Polypeptide GalNac Transferase 7/GALNT7 protein
Leu28-Val657, with a C-terminal 6-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

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

N-terminal Sequence Analysis

Leu28 & Asp46

Predicted Molecular Mass

73 kDa

SDS-PAGE

60-70 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 >800 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

7748-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 7/GALNT7

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). GALNT7 has a restricted preference for glycopeptides, i.e. requiring substrates that have been already decorated with GalNAc by other GALNTs, and has little redundant activity from the other family members (7, 8). Human GALNT7 is expressed in uterus, retina, kidney, small intestine, stomach and central nervous system (8). Recently, GALNT7 was identified as an oncogenic target in cervical cancer (9). The enzymatic activity of recombinant human GALNT7 was determined using a phosphatase-coupled assay (10).

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. Bennett, E. P. et al. (1999) FEBS Lett. 460:226.
  8. Perrine, C.L. et al. (2009) J. Biol. Chem. 284:20387.
  9. Peng, R.Q. et al. (2012) J. Biol. Chem. 287:14301.
  10. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 7

Alternate Names

GALNAC-T7, GalNAcT7, pp-GaNTase 7

Entrez Gene IDs

51809 (Human); 108150 (Mouse); 29750 (Rat)

Gene Symbol

GALNT7

UniProt

Q86SF2 (Human)

Additional Polypeptide GalNAc Transferase 7/GALNT7 Products

Product Documents for Recombinant Human GALNT7 Protein, CF

Product Datasheets

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Product Specific Notices for Recombinant Human GALNT7 Protein, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

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