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Recombinant Human B3GALNT2 Protein, CF

Catalog # 1848-GT | R&D Systems, Inc. a Bio-Techne Brand
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Key Product Details

Accession #






Enzyme Activity

Product Specifications


Chinese Hamster Ovary cell line, CHO-derived human B3GALNT2 protein
Gly35-Arg500, with C-terminal 6x His tag


>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


Predicted Molecular Mass

54 kDa


55-63 kDa, reducing conditions


Measured by its ability to transfer GalNAc from UDP-GalNAc to benzyl-GlcNAc.
The specific activity is >10 pmol/min/ μg, as measured under the described conditions

Formulation, Preparation and Storage

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: B3GALNT2

B3GALNT2 was first identified in 2004 through a BLAST search (1). The expressed B3GALNT2 strictly transferred GalNAc to terminal GlcNAc residue and synthesized a unique carbohydrate structure GalNAc-beta 1,3-GlcNAc, which was not known in humans or other mammals previously. The related native structure was only found later in a study of congenital muscular dystrophies (CMD), a heterogeneous group of inherited diseases characterized by the onset of muscle weakness at birth or within 2 years of life. A common subgroup within the CMDs are the dystroglycanopathies, characterized by reduced functional glycosylation of alpha-dystroglycan ( alpha-DG), a peripheral membrane protein that binds to several extracellular matrix components. Proper glycosylation of alpha-DG is critical to maintain structural integrity and force transmission between the cytoskeleton and the extracellular matrix for efficient signal transduction. Deleterious mutation in gene of B3GALNT2 was found in some of the patients of dystroglycanopathies (2). The complete structure of B3GALNT2 product was then found as an O-mannosyl trisaccharide GalNAc-beta 1,3-GlcNAc-beta 1,4-Man (3) with the mannose phosphorylated at the 6-position (4). The enzymatic activity of recombinant human B3GALNT2 was determined using a phosphatase-coupled assay (5) using GlcNAc beta1-O-benzyl as acceptor substrate. Recombinant B3GALNT2 is also found to be highly active and specific towards O-GlcNAc and therefore is an ideal enzyme for the detection and labeling of O-GlcNAc (6). O-GlcNAc is a single GlcNAc residue attached to serine/threonine residues on nuclear and cytosolic proteins with regulatory roles from transcription, translation, cell signaling to cell cycle regulation (7).


  1. Hiruma, t, et al. (2004) J. Biol. Chem. 279:14087.
  2. Stevens, E. et al. (2013) Am. J. Hum. Genet. 92:354.
  3. Yoshida-Moriguchi, T. et al. (2013) Science 341:6148.
  4. Yoshida-Moriguchi, T. et al. (2010) Science 327:88.
  5. Wu, Z.L. et al. (2011) Glycobiology 21:727.
  6. Wu, Z.L. et al. (2018)
  7. Wells L, et al. (2001) Science 291:2376.

Long Name

beta-1,3-N-Acetylgalactosaminyltransferase 2

Alternate Names

B3GalNAc-T2, Beta-1,3-GalNAc-T2, EC 2.4.1, MDDGA11

Entrez Gene IDs

148789 (Human); 97884 (Mouse); 291212 (Rat)

Gene Symbol



Product Documents for Recombinant Human B3GALNT2 Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human B3GALNT2 Protein, CF

For research use only

Setting the standard in quality research reagents