Specific Activity＞80 U/mg;Activity＞50 U/ml for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
Store at 2-8°C Ships Wet ice Check lot-specific COA for exact specifications.
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Product Description
ß-N-acetylglucosaminidase, N-acetyl-β-d-glycosaminide N-acetylglucosaminohydrolase, glucosaminidase, hexosaminidase
N-acetylglucosaminidase cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from complex carbohydrates and glycoproteins.
The cleavage rates of different linkages of GlcNAc on bi-, tri- and tetraantennary oligosaccharides is greatly dependent on the steric hindrance by neighboring residues. The β(1-2)GlcNAc residue linked to the β(1-3)-linked mannose is cleaved at the highest rate and the β(1-2) GlcNAc residue linked to the β(1-6)-linked mannose at the lowest rate for all three oligosaccharides. The β(1-6) GlcNAc residue, when present, is removed at the second highest rate and the β(1-4) GlcNAc, third. On a triantennary structure, this residue is removed at the second highest rate. A bisecting β(1-4) GlcNAc linked to the β-linked mannose severely hinders cleavage of other GlcNAc residues–high concentrations of enzymes and prolonged incubation times are required for cleavage.
Specifictity Cleaves all non-reducing terminal Beta-linked N-acetylglucosamine. Bisecting GlcNAc slows the reaction.
Source recombinant from Streptococcus pneumoniae in E. Coli.
Purity:Each lot of N-acetylglucosaminidase is tested for contaminating protease as follows; 10 μg of denatured BSA is incubated for 24 hours with 2 μL of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation.
EC 3.2.1.52
Specific Activity >80 U/mg
Activity >50 U/ml
Molecular weight ~140,000 daltons
pH range 5-7, optimum 5.0
Specific Activity:Assay Defined as the amount of enzyme required to produce 1 µmole of p-nitrophenol in 1 minute at 37˚C, pH 5.0 from p-nitrophenyl-Beta-D-N-acetyl-glucosaminide
Contents
N-acetylglucosaminidase in 20 mM Tris-HCl, 25 mM NaCl, pH 7.5
Included with 20 µL and 60 µL pack sizes:
5x Reaction Buffer 250 mM sodium phosphate, pH 5.0
Suggested usage
1. Add up to 100 µg of glycoprotein or 1 nmole of oligosaccharide to a tube.
2. Adjust to 14 µl final volume with de-ionized water.
3. Add 4 µl 5x reaction buffer (pH 5.0).
4. Add 2 µl of N-acetylglucosaminidase.
5. Incubate 3 hours at 37˚C.
NOTE: If bisecting GlcNAc or beta(1-2)GlcNAc-alpha(1-6)Man are present increase incubation nation time to 18 hours.
Storage
Store enzyme at 4˚C.
Stability Stable at least 12 months when stored properly. Several days exposure to ambient temperatures will not reduce activity.
The production host strain has been extensively tested and does not produce any detectable glycosidases.
Comprehensive hazard, handling, storage, and regulatory compliance document.
Download SDS →Lot-specific quality data. Enter your lot number to retrieve the exact COA.
Look up COA →Full quality attributes and acceptance criteria for this grade.
View spec sheet →
