Endo and Exoglycosidases for Antibody Glycan Analysis

Use of the endoglycosidic enzyme PNGase F (N-Glycosidase F) is the most common method of removing virtually all N-linked oligosaccharides from glycoproteins. PNGase F cleaves all asparagine-linked complex, hybrid, or high mannose oligosaccharides unless the core contains an a(1?3)-fucose. A tripeptide with the oligosaccharide-linked asparagine as the central residue is the minimal substrate for PNGase F (see Figure 1). The asparagine residue from which the glycan is removed is deaminated to aspartic acid. IgGZERO is highly specific for the N-linked glycan on the CH2 domain of IgG. In addition to iGG specificity, IgGZERO differs from PNGase F in that it cleaves between the two β-D-N-Acetylglucosamines of the glycan′s chitobiose core.

Enzymatic analysis of oligosaccharides using highly specific exoglycosidases, either sequentially or in a matrix array, is a powerful technique in determining the sequence and structure of glycans. Exoglycosidases remove terminal carbohydrates from the non-reducing end of a glycan, but do not cleave internal bonds between carbohydrates. By using positionally specific exoglycosidases, the removed glycan residues can be identified by linkage as well as sugar. For example, β(1-4) galactosidase will remove terminal β-galactose residues attached with a (1-4) linkage but not residues attached with a (1-3) or (1-6) linkage. In glycan sequencing, the glycan pool is separated into individual oligosaccharides, and each purified glycan is digested sequentially with various linkage-specific exoglycosidase enzymes. For more information visit the Glycobiology Analysis Manual.
Enzymatic analysis of oligosaccharides using highly specific exoglycosidases, either sequentially or in a matrix array, is a powerful technique in determining the sequence and structure of glycans. Exoglycosidases remove terminal carbohydrates from the non-reducing end of a glycan, but do not cleave internal bonds between carbohydrates. By using positionally specific exoglycosidases, the removed glycan residues can be identified by linkage as well as sugar. For example, ß(1?4) galactosidase will remove terminal ß-galactose residues attached with a (1?4) linkage but not residues attached with a (1?3) or (1?6) linkage. In glycan sequencing, the glycan pool is separated into individual oligosaccharides, and each purified glycan is digested sequentially with various linkage-specific exoglycosidase enzymes. For more information visit the Glycobiology Analysis Manual.
IgGZERO has a specific endoglycosidase activity on native IgG by hydrolyzing the conserved glycans

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A2415 β-N-Acetylglucosaminidase from bovine kidney ammonium sulfate suspension, 10-50 units/mg protein
A2264 β-N-Acetylglucosaminidase from Canavalia ensiformis (Jack bean) ammonium sulfate suspension, ≥15 units/mg protein
A6805 β-N-Acetylglucosaminidase from Streptococcus pneumoniae recombinant, expressed in E. coli, buffered aqueous solution
G6920 Endo-β-galactosidase from Bacteroides fragilis recombinant, expressed in E. coli, ≥140 units/mg protein, buffered aqueous solution
E9762 Endoglycosidase F1 from Elizabethkingia miricola recombinant, expressed in E. coli, ≥16 U/mg, buffered aqueous solution
E0639 Endoglycosidase F2 from Elizabethkingia miricola recombinant, expressed in E. coli, 20 U/mg
E2264 Endoglycosidase F3 from Elizabethkingia miricola recombinant, expressed in E. coli, 30 U/mg
E7642 Endoglycosidase H from Streptomyces plicatus recombinant, expressed in E. coli, buffered aqueous solution
A0810 Endoglycosidase H from Streptomyces plicatus recombinant, expressed in E. coli, buffered aqueous solution
F9272 α-1,2-Fucosidase solution buffered aqueous solution
F1924 α-1→(2,3,4)-Fucosidase solution from Xanthomonas sp. buffered aqueous solution
F3023 α-1→(3,4)-Fucosidase solution from Xanthomonas sp. buffered aqueous solution
F6272 α-1,6-Fucosidase solution from Elizabethkingia miricola recombinant, expressed in E. coli, buffered aqueous solution
G3153 β-Galactosidase from Escherichia coli lyophilized powder, ≥500 units/mg protein
G1288 β-(1→3,4,6)-Galactosidase, positionally specific recombinant, expressed in E. coli, buffered aqueous solution
G0288 β-(1→3,6)-Galactosidase, positionally specific from Xanthomonas manihotis recombinant, expressed in E. coli, buffered aqueous solution
G0413 β(1→4)-Galactosidase, positionally specific from Streptococcus pneumoniae recombinant, expressed in E. coli, buffered aqueous solution
G7163 α-Galactosidase, positionally specific from Escherichia coli recombinant, expressed in E. coli, buffered aqueous solution
G0535 Glycopeptidase A from almonds buffered aqueous glycerol solution, ≥0.05 unit/mL
G1163 O-Glycosidase from Streptococcus pneumoniae recombinant, expressed in E. coli, buffered aqueous solution
M7257 α-Mannosidase from Canavalia ensiformis (Jack bean) ammonium sulfate suspension, ≥15 units/mg protein (biuret)
M9400 β-Mannosidase from Helix pomatia 5-30 units/mL, ammonium sulfate suspension, crude extract
N2133 Neuraminidase from Clostridium perfringens (C. welchii) Type X, lyophilized powder, ≥50 units/mg protein (using 4MU-NANA)
N7271 α(2→3) Neuraminidase from Streptococcus pneumoniae buffered aqueous solution
N5521 α(2→3,6) Neuraminidase from Clostridium perfringens (C. welchii) recombinant, expressed in E. coli, buffered aqueous solution, ≥250 units/mg protein
N3786 α(2→3,6,8,9) Neuraminidase from Arthrobacter ureafaciens Proteomics Grade, suitable for MALDI-TOF MS
N8271 α(2→3,6,8,9) Neuraminidase from Arthrobacter ureafaciens recombinant, expressed in E. coli, buffered aqueous solution
G5166 PNGase F from Elizabethkingia miricola buffered aqueous solution
P7367 PNGase F from Elizabethkingia meningoseptica BioReagent, ≥95% (SDS-PAGE), for proteomics
P9120 PNGase F from Elizabethkingia meningoseptica recombinant, expressed in E. coli, set of 100 units nanomolar unit
F8435 PNGase F from Elizabethkingia meningoseptica lyophilized powder, recombinant, expressed in E. coli
G1549 PNGase F from Elizabethkingia meningoseptica buffered aqueous solution, recombinant, expressed in E. coli