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α(2-3) Neuraminidase from Salmonella typhimurium LT2, Recombinant

Cat No.
NATE-1276
Description
Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions.
Abbr
α(2-3) Neuraminidase, Recombinant (Salmonella typhimurium LT2)
Source
E. coli
Species
Salmonella typhimurium LT2
Product Overview
α2-3 Neuraminidase is a highly specific exoglycosidase that catalyzes the hydrolysis of α2-3 and, at a much lower rate, α2-6 linked N-acetyl-neuraminic acid residues from oligosaccharides. This enzyme has a 260-fold preference for α2-3 sialyl linkages over α2-6 sialyl linkages and shows only trace activity against α2-8 sialyl linkages.
Form
50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C), and 5 mM Na2EDTA.
Activity
~11,300,000 units/mg
Molecular Weight
41 kDa
Concentration
50,000 units/ml
Unit Definition
One unit is defined as the amount of enzyme required to cleave > 95% of the αNeu5Ac from 1 nmol of Neu5Acα2-3Galβ1-3GlcNAcβ1-3Galβ1-4Glc-7-amino-4-methyl-coumarin (AMC), in 1 hour at 37°C in a total reaction volume of 10 µl.
Storage
Store at 4°C or in small aliquots at –20°C. Avoid repeated freeze/thaw cycles.
Synonyms
neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6
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