Sialidase Cp Alpha-(2-3,6)

- Overview
  - α(2-3,6) Sialidase Cp cleaves all non-reducing terminal non-branched α(2-3) and α(2-6) sialic acid residues from complex carbohydrates and glycoproteins. There is no detectable activity on α(2-8) or α(2-9) linkages or on branched α(2-3) or α(2-6) linkages. The relative cleavage rates for different linkages are: α(2-3) > α(2-6).
    
    α(2-3,6) Sialidase Cp will not cleave branched sialic acids (linked to an internal residue). Use α(2-3,6,8,9) Sialidase Au (E-S001) for α(2-8) or branched sialic acids. To cleave only non-reducing terminal α(2-3) unbranched sialic acid residues, use α(2-3) Sialidase Sp (E-S007).
    
    α(2-3,6) Sialidase Cp is isolated from a clone of Clostridium perfringens. The enzyme has been extensively characterized using oligosaccharide standards.
    
    Contents:
    Sialidase Cp in 20 mM Tris-HCl, 25 mM NaCl, pH 7.5
    5x Reaction Buffer 250 mM sodium phosphate, pH 6.0
    
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    Glycosidases
- Properties
  - Name
    
    Neuraminidase, NANase, N-acetylneuraminate glycohydrolase, Exo-α-sialidase
    
    Source
    
    Recombinant from Clostridium perfringens in E. coli.
    
    Storage
    
    Store enzyme at 4°C.
    
    Activity
    
    >15 U/mL
    
    More Information
    
    Database Link
    
    EC 3.2.1.18
    
    * For research use only
- Applications
  - Application
    
    Glycan Release
- Reference
  - 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. Biochem 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. 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).
    5. Uchida, Y., Y. Tsukada and T. Sugimori. Enzymatic properties of neuraminidases from Arthrobacter ureafaciens. J Biochem (Tokyo) 86: 573-58 5 (1979).
    6. Roggentin, P, B. Rothe, F Lottspeich and R. Schauer. Cloning and sequencing of a Clostridium perfringens sialidase gene. FEBS Lett 238: 31-34 (Se pt 1988).
    7. Roggentin P., R.G . Kleineidam and R. Schauer. Diversity in the properties of two sialidase isoenzymes produced by Clostridium perfringens spp. Biol Chem Hoppe-Seyler 376: 569-575 (1995)

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Sialidase Cp Alpha-(2-3,6)

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