Alpha-(1-2,3,6)-Mannosidase (Alpha-D-Mannoside Mannohydrolase)

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

The kit contains reagents for the release of N and O-linked glycans from glycoproteins via hydrazinolysis.

α(1-6) Core Mannosidase cleaves unbranched non-reducing terminal mannose, α(1-6) linked to the β-linked core mannose of the conserved mannosylchitobiose core of N-linked oligosaccharides.  The presence of fucose linked to the core N-acetylglucosamine does not affect cleavage.

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.

For the release of O-linked glycans from glycoprotein therapeutics.

α(1-3,4) Fucosidase cleaves branched non-reducing terminal fucose, linked α(1-3) or α(1-4) to the N-acetylglucosamine of terminal Gal-GlcNAc disaccharide structures. The presence of sialic acid (but not fucose) linked to the galactose will block cleavage.

Non-reducing terminal β(1-4)-Galactose. The number of antennae does not affect cleavage rate. Fucose linked to the penultimate N-acetylglucosamine will block the cleavage of the galactose.

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.

N-acetylglucosaminidase cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from complex carbohydrates and 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.

α(2-3,6,8,9) Sialidase Au cleaves all cleaves all non-reducing terminal sialic acid residues from complex carbohydrates and glycoproteins. The relative cleavage rates for different linkages are: α(2-6) > α(2-3) > α(2-8), α(2-9).

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.

α(2-3,6) Sialidase Cp cleaves all non-reducing terminal non-branched α(2-3) and α(2-6) sialic acid residues from complex carbohydrates and glycoproteins. There is no detectable activity on α(2-8) or α(2-9) linkages or on branched α(2-3) or α(2-6) linkages. The relative cleavage rates for different linkages are: α(2-3) > α(2-6).

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.

Sialidase Sp cleaves the non-reducing terminal α(2-3) unbranched sialic acid residues from complex

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.

To remove 9-, 8- and 7-O-acetyl groups from released sialic acids, released glycans or glycoproteins. Used for characterisation of highly sialylated biotherapeutics such as EPO, FSH and blood clotting factors. Kit includes enzyme plus reaction buffer. Sufficient for up to 50 samples.

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.

LudgerZyme PNGase L is a recombinant glycoglycoamidase cloned from Flavobacterium akiainvivens.