Sialidase Au Alpha-(2-3,6,8,9)

Sialidase Au Alpha-(2-3,6,8,9)

Catalog Number:
E001088474LUD
Mfr. No.:
E-S001
Price:
$525
  • Size:
    0.3 U/60 µL
    Quantity:
    Add to Cart:
      • Overview
        • α(2-3,6,8,9) Sialidase 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 sialidases. 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 Sialidase SP, part number E-S007.

          α(2-3,6,8,9) Sialidase Au is isolated from a clone of Arthrobacter ureafaciens. The enzyme has been extensively characterized using oligosaccharide standards.

          Contents:
          Sialidase Au in 20 mM Tris-HCl, 25 mM NaCl, pH 7.5
          5x Reaction Buffer 250 mM sodium phosphate, pH 6.0

          Please contact us at for specific academic pricing.

          More Details

      • Properties
        • Name
          Neuraminidase, NANase, N-acetylneuraminate glycohydrolase, Exo-α-sialidase
          Source
          Recombinant from Arthrobacter ureafaciens in E. Coli.
          Purification
          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. The production host strain has been extensively tested and does not produce any detectable glycosidases.
          Storage
          Store enzyme at 4°C.
          Note
          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.
          Activity
          >5 U/mL

          More Information

          Database Link

          * 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. 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. Ohta, Y., Y. Tsukada and T. Sugimori. Purification and properties of neuraminidase isoenzymes in Arthrobacter ureafaciens mutant. J Biochem (Tokyo) 106: 1086- 1089 (1989).
          5. 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).
          6. Uchida, Y., Y. Tsukada and T. Sugimori. Enzymatic properties of neuraminidases from Arthrobacter ureafaciens. J Biochem (Tokyo) 86: 573-58 5 (1979).

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