Specific Activity ＞135 U/mg;Activity＞5 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
Sialidase, NANase, N-acetylneuraminate glycohydrolase, Exo-alpha-sialidase
α (2-3,6,8,9) Neuraminidase 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).
In addition, the enzyme will cleave branched sialic acids (linked to an internal residue). This property makes it unique among neuraminidases. High concentrations of enzymes and prolonged incubation times may be required for cleaving branched residues. To cleave only non- reducing terminal α(2-3) unbranched sialic acid residues, use Neuraminidase SP, part number E-S007.
α-(2-3,6,8,9) Neuraminidase is isolated from a clone of Arthrobacter ureafaciens. The enzyme has been extensively characterized using oligosaccharide standards.
Purity Each lot of α(2-3,6,8,9) Neuraminidase 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.
Source recombinant from Arthrobacter ureafaciens in E. Coli.
EC 3.2.1.18
Specific Activity >135 U/mg
Activity>5 U/ml
Molecular weight 70,000 daltons
pH range 4.5-7, optimum 6.0
The recommended buffer concentrate provides the optimal pH for enzyme activity with the standard substrate. If glycosidase treatment is performed at suboptimal pH because of glycoprotein solubility or activity requirements, expect some diminution in enzyme activity.
Specific Activity Defined as the amount of enzyme required to produce 1 µmole of methylumbelliferone in 1 minute at 37˚C, pH 5.0 from MU-NANA [2′-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid].
Contents
Neuraminidase 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 6.0
Suggested usage
1. Add up to 100 μg of glycoprotein or 1 nmol of oligosaccharide to tube.
2. Add water to 14 μL
3. Add 4 μL 5X Reaction Buffer.
4. Add 2 μL α (2-3, 6,8,9) Neuraminidase.
5. Incubate at 37°C for 1 hour.
Desialylation may be monitored by SDS-PAGE if the size differential between native and desialylated protein is sufficient for detection.
NOTE: longer incubation times are necessary if branched sialic acids are present.
Specifictity Cleaves all non-reducing terminal branched and unbranched sialic acids
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. Enzyme remains active at 37˚C for at least one week.
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.
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