Ludger Sialidase Sp enzyme structure

    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

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








    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:
    Ludger Sialidase Sp - Kit 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).