Endoglycosidases



Endoglycosidase H

Endoglycosidase H [Endo-β-N-acetylglucosaminidase H, EC 3.2.1.96] cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins (see Figure). It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose 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.

5 U/ml - 300 mU for 60 μL

GE44 datasheet pdf



Endoglycosidase F1

Endoglycosidase F1 [Endo-β-N-acetylglucosaminidase F1, EC 3.2.1.96] cleaves asparagine-linked or free oligomannose and hybrid, but not complex, oligosaccharides (see figure 1). Core fucosylation reduces the activity by 50 fold. Endoglycosidase F1 will hydrolyze sulfate containing high-mannose chains. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose 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.

17 U/ml - 1 U for 60 μL

GE47 datasheet pdf



Endoglycosidase F2

Endoglycosidase F2 [Endo-β-N-acetylglucosaminidase F2 EC 3.2.1.96] cleaves asparagine-linked or free oligomannose and biantennary complex, oligosaccharides (see Figure 1). It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose 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.

5 U/ml - 300 mU for 60 μL

GE48 datasheet pdf


Endoglycosidase F3

Endoglycosidase F3 [Endo-β-N-acetylglucosaminidase F3, EC 3.2.1.96] cleaves asparagine-linked biantennary and triantennary complex, oligosaccharides depending on the state of core fucosylation and peptide linkage (see Figure 1). It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose 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.. There is no activity on oligomannose and hybrid molecules.

5 U/ml - 300 mU for 60 μL

GE49 datasheet pdf


Endo-β-Galactosidase
Recombinant from Bacteroides fragilis

Endo-β-Galactoctosidase(EC 3.2.1.103) 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.

15 U/ml - 900 mU for 60 μL

GE38 datasheet pdf


Endo-α-N-acetylgalactosaminidase(Endo-O-Glycosidase)

Endo-O-glycosidase (O-glycopeptide endo-D-galactosyl-N-acetyl-α-galactosaminohydrolase, EC 3.2.1.97) cleaves only unsubstituted Galβ(1-3)-GalNAcα disaccharides attached to the serine or threonine residues of glycoproteins or glycopeptides. Substitutions such as sialic acid, fucose, galactose or N-acetylglucosamine must first be removed with the appropriate exoglycosidase prior to treatment with Endo-O-Glycosidase. At minimum, a sialidase such as GE 23, from Arthrobacter ureafaciens is almost always required to remove sialic acid.

1.25 U/ml - 75 mU for 60 μL


GE43 datasheet pdf