Recombinant human Polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2), soluble fragment



Polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2) catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the hydroxyl group of serine and threonine residues (1).  Twenty GalNAc-T genes have been identified in humans and most have been shown to represent active GalNAc-Ts.  All isoforms are type II transmembrane proteins, with different but partly overlapping substrate preferences (2).  The GalNAc-Ts control the initiation of mucin-type O-linked glycosylation and determine the location and density of O-glycans in a protein (2).  Addition of GalNAc to an unglycosylated Ser/Thr residue creates the Tn antigen GalNAca1-S/T, and subsequent addition of sialic acid by ST6GalNAc-I forms the cancer associated STn antigen (3).  GalNAc-T2 is primarily located in Golgi, and is widely distributed in human tissues (1,4,5).

  • White, T. et al. (1995) J. Biol. Chem. 270, 24156.
  • Tian, E. & Ten Hagen, K.G. (2009) Glycocon. J. 26, 325.
  • Sewell, R. et al. (2006) J. Biol. Chem. 281, 3586.
  • Röttger, S. et al. (2011) J. Cell Sci. 111, 45.
  • Gill, D.J. et al. (2011) Trends Cell Biol. 21, 149.

Catalog #:  SBH-003-GalNAc-T2

Source :  Insect Cells, Accession # Q10471

Formulation:  Sterile filtered solution in 20mM Hepes pH7 and 100mM NaCl, at a stock concentration of 360 ug/mL.

Stability:  Stable for 4 weeks at 4C.  Stable for 6 months at -80C.  Avoid repeated freeze-thaw cycles.

Purity:  Greater than 90% by SDS-PAGE.

Reconstitution:  N/A

Biological Activity:  Measured by transfer of GalNAc from UDP-GalNAc to the peptide MEELGMAPALQPTQGAMPAF, enzyme reactions containing: 25mM Caco pH 7.4, 10mM MnCl, 0.25% Triton X100, 2mM UDP-GalNAc and 10mg (400ug/mL final) peptide. Incubated at 37ºC.  Specific activity > 300 pmol/min/mg.  Specific activity > 300 pmol/min/ug.

PubMed  Link: GalNAc-T2 Human

Usage:  For research only. Not for use in diagnostic or therapeutic procedures.

Country of Origin:  USA


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