N-Glycosidase A

N-Glycosidase A has been used to selectively deglycosylated chondroitin sulfate proteoglycans (CSPGs).

N-Glycosidase A is an amidase and cleaves N-glycans between asparagine and the carbohydrate chain, converting asparagine to aspartic acid. The enzyme is used to isolate intact oligosaccharide and peptide moieties for structural analysis and functional examination of each moiety.

Use N-Glycosidase A to cleave glycopeptides. The enzyme cleaves all types of asparagine-bound N-glycans including high mannose-, hybrid-, biantennary-, triantennary- and tetraantennary complex types, provided that the amino-group as well as the carboxyl-group are present in the peptide linkage. N-Glycosidase A can also cleave a single N-acetylglucosamine residue from the peptide, albeit at a slower reaction rate.
The oligosaccharide is first released as a glycosylamine, which hydrolyzes spontaneously under the acidic conditions of the reaction to the reducing end containing glycan and to ammonia.
In contrast to N-Glycosidase F from Flavobacterium meningosepticum, N-Glycosidase A from almonds can degrade N-linked glycans carrying a fucose linked α(1-3) to Asn-GlcNAc. This structural motif is present in plant glycoproteins and is also found in insect glycoproteins.

Hydrolyzes all types of N-glycan chains from glycopeptides, even those carrying α1,3-bound core fucose residues present in insect and plant glycoproteins.

Solution in 50 mM citrate/phosphate buffer, glycerol, 50 % (v/v), pH 5.0

Contaminating activities like a- and β-galactosidase, α- and β-mannosidase, β-glucosidase, β-N-acetylhexosaminidase, α-L-fucosidase, β-xylosidase and sialidase are below 0.1%. Protease activitiy is not detectable, according to the current quality control procedures.

For life science research only. Not for use in diagnostic procedures.

One unit is the enzyme activity that hydrolyzes 1 μmol ovalbumin glycopeptide Glu-Glu-Lys-Tyr-Asn-(CHO)-Leu-Thr-Ser-Val within 1 minute at 37 °C at pH 5. CHO consists of hybrid- and high-mannose type oligosaccharides.

The sale of the Product does not exhaust or grant any rights in third party patents including patents of companies of the F. Hoffmann - La Roche AG group of companies, in particular, for the use of modified antibodies obtained by using the product.