Recombinant E. faecalis O-Glycosidase Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 8886-GH

R&D Systems, part of Bio-Techne
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8886-GH-020
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Key Product Details

Source

E. coli

Accession #

Q833X5

Conjugate

Unconjugated

Applications

Enzyme Activity

View all O-Glycosidase Proteins and Enzymes »

Product Specifications

Source

E. coli-derived e. faecalis O-Glycosidase protein
Glu29-Lys1324, with N-terminal Met and 6-His tag

Purity

>75%, 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

Met

Predicted Molecular Mass

145 kDa

SDS-PAGE

128 kDa, reducing conditions

Activity

Measured by its ability to hydrolyze p-Nitrophenyl galacto-N-bioside.
The specific activity is >12,500 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

8886-GH
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: O-Glycosidase

Enterococcus faecalis O-Glycosidase, also known as endo-alpha -N-Acetylgalactosaminidase, removes O-glycans from glycoproteins. It is broadly active on Core-1, Core-2, Core-3 and Gal-Core-2 structures, which releases the following oligosaccharides, Gal beta1-3GalNAc, Gal beta1-3[GlcNAc beta1-6]GalNAc, GlcNAc beta1-3GalNAc, Gal beta1-3[Gal beta1-3GlcNAc beta1-6]GalNAc, respectively (1). The enzyme is most active on Core 1, followed by Core 3, then Core 2 structures. The enzyme also has transglycosylation activity and can transfers Core-1 and Core-2 glycans to 1-alkanols, generating alkyl-oligosaccharides. Because the O-Glycosidase is not active on sialylated O-glycans, it is necessary to treat glycoproteins concomitantly with a neuraminidase for deglycosylation purpose (2).

References

  1. Goda, H. M. et al. (2008) Biochem Biophys Res Commun 375:441.
  2. Koutsioulis, D. et al. (2008). Glycobiology 18:799.

Alternate Names

Endo-alpha-N-Acetylgalactosaminidase, OGlycosidase

UniProt

Q833X5

Additional O-Glycosidase Products

Product Documents for Recombinant E. faecalis O-Glycosidase Protein, CF

Product Datasheets

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Product Specific Notices for Recombinant E. faecalis O-Glycosidase Protein, CF

For research use only

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