Endo F1 cleaves high mannose and some hybrid type N-glycans from peptides and proteins.

Endo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It also will cleave high mannose glycans but at a 40x reduced rate. It cleaves between the two N-acetylglucosamine residues in the diacetyl chitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact.

Selective release of triantennarry and α(1-6) fucosylated biantennary N-glycans from peptides and protein.

Endo H cleaves Asparagine-linked hybrid or high mannose oligosaccharides, but not complex oligosaccharides. It cleaves between the two N-acetylglucosamine residues in the diacetyl chitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Detergent and heat denaturation may increase the rate of cleavage for some glycoproteins.

O-glycosidase cleaves only unsubstituted Gal-β(1-3)GalNAc-α disaccharides attached to the serine or threonine residues of glycoproteins or glycopeptides.

PNGase F is suitable for the release of all types (high-mannose, hybrid and complex) N-linked glycans from glycoproteins and glycopeptides. PNGase F will not remove oligosaccharides containing α(1-3) linked core fucose commonly found on plant glycoproteins.

PNGase F is suitable for the release of all types (high-mannose, hybrid and complex) N-linked glycans from glycoproteins and glycopeptides. PNGase F will not remove oligosaccharides containing α(1-3) linked core fucose commonly found on plant glycoproteins.

PNGase F is suitable for the release of all types (high-mannose, hybrid and complex) N-linked glycans from glycoproteins and glycopeptides. PNGase F will not remove oligosaccharides containing α(1-3) linked core fucose commonly found on plant glycoproteins.

Endo-β-Galactosidase cleaves internal β(1-4) galactose linkages in unbranched, repeating poly-N-acetyllactosamine structures. Sulfated structures such as keratan sulfate are also cleaved. Branching and/or fucosylation of the substrate may decrease or eliminate cleavage.

This kit includes the enzymes and buffers required to deglycosylate glycoproteins, removing all N-linked oligosaccharides and many O-linked sugars.

This kit developed for protein deglycosylation includes our DeGlycoMx, a premixed cocktail of the enzymes required to remove all N-linked oligosaccharides and most O-linked sugars from 0.5 mg of glycoprotein, via 10 reactions of up to 50 micrograms of protein per reaction.

Ceramide glycanase can be used to deglycosylate a variety of glycosphingolipids by cleaving the β-glycosyl linkage. Ceramide glycanase allows the identification of glycosylation patterns of glycosphingolipids through cleaving the glycan moiety and making it accessible to LudgerTag labelling technology.