- Part Number
- E-S007
- Amount of Enzyme
- 0.3 U / 60 µL

Sialidase Sp α(2-3)
E-S007
Sialidase Sp cleaves the non-reducing terminal α(2-3) unbranched sialic acid residues from complex carbohydrates and glycoproteins.
View product documentation: Specsheet / CofA / MSDS
Kit includes enzyme plus reaction buffer.
Sufficient for up to 60 reactions.
Product Specifications:
α(2-3) Sialidase Sp cleaves exclusively the non-reducing terminal α(2-3) unbranched sialic acid residues from complex carbohydrates and glycoproteins. There is no detectable activity on α(2-6) or α(2-8) linkages or on branched α(2-3) linkages. To cleave all non-reducing terminal sialic acid residues including branched sialic acids (linked to an internal residue) from complex carbohydrates and glycoproteins, use α(2-3,6,8,9) Sialidase Au (E-S001).
Source: Recombinant Streptococcus pneumoniae in E. coli
EC: 3.2.1.18
Alternate Names: Neuraminidase, N-acetylneuraminate glycohydrolase, Exo-α-sialidase
Contents:
Sialidase Sp in 50 mM sodium phosphate, pH 7.5
5x Reaction Buffer 250 mM sodium phosphate, pH 6.0
Specific Activity: = 250 U/mg
Activity: = 10 U/mL
Molecular weight: ~75,000 daltons
pH optimum 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) Sialidase Sp.
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.
Specificity: Cleaves the non-reducing terminal α(2-3) unbranched sialic acid residues from complex carbohydrates and glycoproteins.
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].
Storage Store enzyme at 4°C.
Companion Products:
Process controls - View our N-glycan Nomenclature Table
- CAB-STP-NEUAC-01
- CPROC-STP-NEUAC-01
- Sialidase Test Panel - mix of 2-AB labelled glycans with different NeuAc linkages *Coming Soon
- Sialidase Test Panel - mix of procainamide labelled glycans with different NeuAc linkages *Coming Soon
Glycan clean-up - removal of enzymes from glycan mixtures following exoglycosidase treatment
- LC-EXO-A6
- LC-EXO-96
- LudgerClean Post-Exoglycosidase Clean-up Spin Columns (6 samples)
- LudgerClean Post-Exoglycosidase Clean-up Plate (96 samples)
Labelling and derivatisation of released glycans - View our Glycan Labelling Summary Table
- LT-KAB-A2
- LT-KAB-VP24
- LT-KAB-VP96
- LT-KPROC-24
- LT-KPROC-96
- LT-KPROC-VP24
- LT-KAA-A2
- LT-KAA-VP24
- LT-PERMET-96
- LT-PERMET-VP96
- LudgerTag 2-AB Glycan Labelling Kit, sodium cyanoborohydride (24 samples)
- LudgerTag 2-AB Glycan Labelling Kit, picoline borane (24 samples)
- LudgerTag 2-AB Glycan Labelling Kit, picoline borane (96 samples)
- LudgerTag Procainamide Glycan Labelling Kit, sodium cyanoborohydride (24 samples)
- LudgerTag Procainamide Glycan Labelling Kit, sodium cyanoborohydride (96 samples)
- LudgerTag Procainamide Glycan Labelling Kit, picoline borane (24 samples)
- LudgerTag 2-AA Glycan Labelling Kit, sodium cyanoborohydride (24 samples)
- LudgerTag 2-AA Glycan Labelling Kit, picoline borane (24 samples)
- LudgerTag Permethylation Kit (96 samples)
- LudgerTag Permethylation Kit, without methyl iodide (96 samples)
Alternative enzymes
- E-S001
- E-S005
- LZ-ACASE-KIT
- Sialidase Au α(2-3,6,8,9)
- Sialidase Cp α(2-3,6)
- Acetyl esterase (sialate-O-acetylesterase), removal of O-acetyl groups from sialic acids
References:
1. Corfield, A. P., H. Higa, J. C. Paulson and R. Schauer. The specificity of viral and bacterial sialidases for alpha(2-3) and alpha(2-6)-linked sialic acids in glycoproteins. Biochim Biophys Acta 744: 121-12 6 (1983).
2. Dwek, R. A., C. J. Edge, D. J. Harvey, M. R. Wormald and R. B. Parekh. Analysis of glycoprotein-associated oligosaccharides. Ann Rev Biochem 62: 65-100 (1993).
3. Kobata, A. Use of endo- and exoglycosidases for structural studies of glycoconjugates. Anal Biochem 100: 1-14 (1979).
4. Glasgow, L R., J. C . Paulson and R. L. Hill. Systematic purification of five glycosidases from Streptococcus pneumoniae. J. Biol Chem 252: 8615-8623 (1977).
5. Kelly, R. T., D. Greiff and S. Farmer. Neuraminidase activity in Diplococcus pneumoniae. J Bacteriol 91: 601-3 (1965).
6. Prime, S., J. Dearnley , A. M. Venton, R. B. Parekh and C. J. Edge. Oligosaccharide sequencing based on exo- and endoglycosidase digestion and liquid chromatographic analysis of the products. J Chromatogr A 720: 263-274 (1996).