MilliporeSigma

Glycosidases

Glycosidases for your glycobiology workflow needs

Glycosidases, including endoglycosidases and exoglycosidases, are primarily used in glycomics research for the sequencing of glycans, release of N- and O-linked glycans from glycoproteins, and glycoprotein production. Specifically:

  • Glycosidases such as our recombinant Peptide-N-glycosidase F, PNGase Fast, enable complete and rapid deglycosylation of antibodies and immunoglobulin fusion proteins, as well as other glycoproteins, to be prepared for downstream chromatography or mass spectrometry analysis.
  • Polysaccharide lyases and carbohydrate esterases are used to degrade glycosaminoglycans (mucopolysaccharides) and prepare polysaccharide components.
  • Glycosyltransferases are being studied for use in engineering selective glycosylation to improve the therapeutic properties of proteins and antibodies, and to reduce the immunogenicity of xenogenic tissues.

To accommodate your glycobiology workflow needs, we offer a wide range of products for functional and structural analysis of glycans, including glycoprocessing enzymes, glycoproteins, proteoglycans, glycolipids, and free oligosaccharides. This includes offerings of glycan recognizing proteins, including lectins and galectins, and our carbohydrate-active enzymes, covering exoglycosidases, endoglycosidases, glycosyltransferases, and many more. With glycosylation being one of the more common and complex post-translational modifications, our GlycoProfile™ kits have been developed for the simple, rapid labeling and analysis of N-glycans and O-glycans of glycoproteins.

Discover even more innovative products for glycomics reagents, kits, and resources below.


Enzymatic Protein Deglycosylation Kit

The Enzymatic Protein Deglycosylation Kits (such as products EDEGLY and NDEGLY) contain all the enzymes and reagents needed to completely remove all N-linked and simple O-linked carbohydrates from glycoproteins. This includes O-linked glycoforms containing galactose, N-acetylglucosamine, and sialic acid. Additional features and benefits include:

  • Deglycosylates up to 2 mg of glycoprotein – Sufficient for downstream processing
  • Single reaction at neutral pH – Retain original peptide structure
  • No protein degradation – Perform interrogation on peptide structure
  • Exoglycosidases included - Processes O-glycoforms for release
  • Removes O-linked sugars containing sialic acid – Get more accurate peptide analysis
  • Control glycoprotein provided – Verification improves confidence and consistency

GlycoProfile™ I Enzymatic In-Gel N-Deglycosylation Kit

The GlycoProfile™ I Enzymatic In-Gel N-Deglycosylation Kit robustly removes N-linked glycans and digests protein samples from 1D- or 2D-polyacrylamide gels for MS or HPLC analysis. The kit works well for Coomassie Brilliant Blue, colloidal Coomassie, and silver stained gels when properly destained. The glycolytic enzyme PNGase F (Peptide-N-Glycosidase F) performs superbly when used for in-gel N-linked deglycosylation of glycoproteins and glycopeptides. Proteomics Grade Trypsin effectively digests the remaining protein. Desalted samples are then concentrated for analysis by MS most commonly using ionization methods such as MALDI or ESI and analyzer methods such as TOF or Quodrupole. This kit offers features and benefits such as:

  • In-gel deglycosylation and digestion – Minimizes sample manipulation
  • Highly purified enzymes – Prevents unwanted activities and byproducts
  • Low buffer salt content – Eliminates interference with MS analysis
  • Destaining reagent included – Saves time by reducing additional reagent preparation

Additional Enzymes for Glycobiology

Complementing our deglycosylation kits, we offer glycolytic enzymes for the removal or partial degradation of glycans. The use of additional enzymes may be useful for certain glycan structures that resist universal deglycosylation strategies, such as structures that PNGase F does not cleave. In addition, sequential hydrolysis of individual monosaccharides from glycans can be used in the analysis of the structure and function of the glycan component.


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