SmartEnzymes OmniGLYZOR workflow

Hydrolysis of N- and Mucin-type O-glycans

OmniGLYZOR contains a mixture of immobilized enzymes for fast and efficient removal of N- and simple mucin-type O-glycans on antibodies, fusion proteins and other glycosylated proteins.

Removal of glycans is widely used to reduce heterogeneity to facilitate analysis of the protein by for example mass spectrometry. Deglycosylation can also be used to study the functional role of the glycans.


  • Fast and efficient deglycosylation of N- and mucin-type O-linked glycans
  • Ready-to-use spin column format - no enzymes interfering in the analysis
  • Compatible with LC-MS
N- and simple mucin-type O-glycans on glycoproteins
1-4 hour reaction
RapiGest™* SF and PNGase F Lyophilized are included
Hydrolysis of N- and simple mucin-type O-glycans, including Tn antigen


A mix of immobilized enzymes in spin columns for deglycosylation of glycoproteins carrying N- and simple O-glycans

About OmniGLYZOR

OmniGLYZOR contains enzymes required for the removal of N-glycans and the most commonly occurring mucin-type O-glycans, namely mono- and disialyl core 1 and Tn antigen (α-GalNAc).

The following activities are included in an OmniGLYZOR Microspin column:

  • PNGase F
  • O-glycosidase
  • Sialidase
  • α-GalNAcase

The glycoprotein sample is incubated with the OmniGLYZOR resin in a microspin column for 1-4 h under native reaction conditions. The deglycosylated glycoprotein is then easily collected by a centrifugation step.


OmniGLYZOR is used for deglycosylation of glycoproteins carrying N- and simple O-glycans.
OmniGLYZOR Kit consists of:

  • OmniGlyZOR Microspin columns
  • PNGase F Lyophilized
  • RapiGest™* SF surfactant

Certain N-glycosylation sites are poorly or not accessible to PNGase F unless the substrate protein is denatured. Remaining N-glycans after incubation on the OmniGLYZOR Microspin column can be removed by an additional deglycosylation step under denaturing conditions using the PNGase F Lyophilized and RapiGest™ SF surfactant included in the kit.

The enzymes hydrolyzing the O-glycans do not benefit from denaturation which is why the OmniGLYZOR columns should only be used under native conditions.

OmniGLYZOR Kit Microspin is provided in kits containing sufficient material to deglycosylate
5 × 50-100 µg or 10 × 50-100 µg glycoprotein.


  • Fast and efficient one-pot deglycosylation of N- and O-linked glycans
  • Compatible with LC-MS
  • Complete removal of glycans for improved analysis of underlying protein
  • Immobilized format increases enzyme-to-substrate ratio to enable fast deglycosylation

Available Products

OmniGLYZOR Kit Microspin 5 x 50-100 𝜇gA mix of immobilized enzymes in spin columns for deglycosylation of 5 x 50-100 𝜇g glycoprotein carrying N- and simple O-glycansG3-OM6-0051,437.00Buy / Request a Quote
OmniGLYZOR Kit Microspin 10 x 50-100 𝜇gA mix of immobilized enzymes in spin columns for deglycosylation of 10 x 50-100 𝜇g glycoprotein carrying N- and simple O-glycansG3-OM6-0102,582.00Buy / Request a Quote

For information on how to order, visit Place an Order or contact us directly at

Unit Definition

One OmniGLYZOR Microspin column contains agarose beads with immobilized enzymes for deglycosylation of 50-100 µg glycoprotein.

Content and Storage

OmniGLYZOR Kit is shipped cold, and the content should be stored at different temperatures upon arrival.

PNGase F Lyophilized and RapiGest SF Surfactant* are provided together with the OmniGLYZOR Microspin columns for optional PNGase F digestion under denaturing conditions.


Product Specification

Safety Data Sheet

Certificate of Analysis

* RapiGest™ SF Surfactant from Waters Corporation is included in OmniGLYZOR Kit. RapiGest™ is a trademark of Waters Corporation.

FAQ and Support

Popular FAQ

No, it is not recommended. We can only guarantee optimal performance for one-time use.

No, both N- and O-glycans are trimmed by the exoglycosidases present in OmniGLYZOR and do not longer represent the structures found on the intact glycoprotein substrate.

OmniGLYZOR hydrolyzes the amide bond between the polypeptide asparagine and the innermost GlcNAc of all mammalian asparagine-linked complex, hybrid, or high mannose oligosaccharides. It does not remove N-glycans with α1-3 core fucosylation.


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