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Sialidase Au α(2-3,6,8,9) [For Glycan Release] (CAT#: CB-P257-K) Datasheet

Product Type
Kit
Description
Α(2-3,6,8,9) sialidase cleaves all non-reducing terminal sialic acid residues from complex carbohydrates and glycoproteins. In addition, the enzyme will also cleave branched sialic acid (and internal The residues are connected).
α(2-3,6,8,9) sialidase Au can cleave all non-reducing terminal sialic acid residues from complex carbohydrates and glycoproteins. The relative cleavage rate of different bonds is: α(2-6)>α(2-3)>α(2-8), α(2-9).

In addition, the enzyme will cleave branched sialic acid (linked to internal residues). This characteristic makes it unique in sialidase. Cleavage of branch residues may require high concentrations of enzymes and extended incubation times. To cut only the non-reducing end α(2-3) unbranched sialic acid residues, use sialidase SP (catalog number CB-P258-K).
α(2-3,6,8,9) sialidase Au was isolated from the clone of Arthrobacter urea. The enzyme has been extensively characterized using oligosaccharide standards.
Features
Source: Recombinant from Arthrobacter ureafaciens in E. Coli.

EC: 3.2.1.18

Alternate Names: Neuraminidase, NANase, N-acetylneuraminate glycohydrolase, Exo-α-sialidase
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.

Specificity: Cleaves all non-reducing terminal branched and unbranched sialic acids

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)-α-D-N-acetylneuraminic acid].

Purity: Each lot of α(2-3,6,8,9) Sialidase Au 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.
Size
0.3 U / 60 µL; Sufficient for up to 60 reactions.
Sample
Glycoproteins and glycopeptides containing N-linked glycans
Components
Sialidase Au in 20 mM Tris-HCl, 25 mM NaCl, pH 7.5
5x Reaction Buffer 250 mM sodium phosphate, pH 6.0
Handling Advice
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) Sialidase Au.
5. Incubate at 37°C for 1 hour.
Storage
Store enzyme at 4°C.
Shelf Life
Stability: Stable at least 12 months when stored properly. Several days exposure to ambient tempertures will not reduce activity.
Research Use
For research use only. Not for human or drug use

All products and services are for Research Use Only. Do Not use in humans.

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