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Cloned alpha 2,3-Sialidase
Cloned alpha 2,3-Sialidase has a 260-fold kinetic preference for the alpha 2,3 sialyl linkage. The enzyme efficiently cleaves sialyl groups from glycoproteins and glycolipids. However, the enzyme may not release sialic acid from O-linked oligosaccharides on glycoproteins.
- This sialidase has a 260-fold kinetic preference for the alpha 2,3 sialyl linkage
- The enzyme efficiently cleaves sialyl groups from glycoproteins and glycolipids
- The enzyme may not release sialic acid from O-linked oligosaccharides on glycoproteins
E. coli (cloned from Salmonella typhimurium LT2)
- Systematic name: Acylneuraminyl hydrolase (E.C. 126.96.36.199)
- Molecular weight: 41.3 kDa (SDS-PAGE)
- Km (substrate):
- 0.25 mM (4MUNeuAc)
- 1.52 mM (3'-sialyliactose)
- 2.66 mM (PA-3'-sialyllactose)
- 2-deoxy-2,3-didehydro-N-acetyl-neuraminic acid
- Ki = 0.38 mM
- Optimum pH:
- pH 5.5–7.0 (Tris-maleate buffer)
- pH 5.5–6.0 (potassium phosphate buffer, sodium acetate buffer, Tris-HCl buffer)
Solution containing 50 mM potassium phosphate (pH 6.8), 0.1 M sodium chloride, and 0.02% sodium azide.
Hoyer, L.L. et al. Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene, nanH, provides evidence for interspecies gene transfer. Mol. Microbiol. 6, 873–884 (1992).
Hoyer, L.L. et al. Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl alpha 2-3 linkages J. Biochem. 110, 462–467 (1991).
Definition of activity
One unit is the amount of enzyme required to hydrolyze 1 µmol of 3'-sialyllactose in 1 minute at 37°C, pH 5.5.
Additional product information
Please see the product's Certificate of Analysis for information about storage conditions, product components, and technical specifications. Please see the Kit Components List to determine kit components. Certificates of Analysis and Kit Components Lists are located under the Documents tab.
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