Sigma-Aldrich Neuraminidase from Vibrio cholerae Type III
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buffered aqueous solution, 0.2 μm filtered, 1-5 units/mg protein (Lowry, using NAN-lactose)
Specifications:
Application | molecular biology | ||
Storage Temperature | 2-8°C | ||
Product Type | Enzymes and Substrates | Forms | Lyophilized |
Product Brand | Sigma-Aldrich | ||
Product Grade | Molecular Biology | ||
Sigma-Aldrich Neuraminidase from Vibrio cholerae, Type III is a high-quality, purified enzyme preparation supplied as a buffered aqueous solution. This enzyme belongs to the glycoside hydrolase family (EC 3.2.1.18) and catalyzes the hydrolysis of terminal sialic acid residues from glycoproteins, glycolipids, and oligosaccharides.
With a specific activity of 1–5 units/mg protein (Lowry, NAN-lactose substrate) and molecular weight of ~83 kDa, this preparation is widely used as a cell-surface probe, in substrate specificity studies, and in diagnostic assay development.
Key Features
- Type III enzyme preparation from V. cholerae.
- Buffered aqueous solution, pH 5.5 with 0.15 M NaCl and 4 mM CaCl₂.
- Chromatographically purified and preservative-free.
- Molecular weight: ~83 kDa.
- Specific activity: 1–5 units/mg protein (Lowry, NAN-lactose).
- Storage temperature: 2–8 °C for stability.
- Foreign activity present: Protease and NAN-aldolase.
Specifications
Parameter | Details |
---|---|
CAS Number | 9001-67-6 |
EC Number (IUBMB) | 3.2.1.18 |
EC Number (EINECS) | 232-624-6 |
MDL Number | MFCD00131711 |
UNSPSC Code | 12352204 |
NACRES | NA.54 |
Form | Buffered aqueous solution |
Molecular Weight | ~83 kDa |
Specific Activity | 1–5 units/mg protein (Lowry, NAN-lactose) |
Unit Definition | 1 unit liberates 1 μmol N-acetylneuraminic acid/min at pH 5.0, 37 °C |
Preservative | None (preservative-free) |
Storage Temp. | 2–8 °C |
Applications
- Diagnostic assay manufacturing – for enzyme-linked assays and research kits.
- Glycoconjugate mapping – used as a probe for analyzing cell-surface glycoconjugate distribution.
- Substrate specificity studies – research into enzyme-substrate interactions.
- Pathogenesis research – study of cholera toxin uptake and infection mechanisms.
- Fluorometric assays – employed in neuraminidase substrate evaluation.
Biochemical/Physiological Actions
- Promotes cholera toxin infection by binding the toxin and aiding its uptake by susceptible cells.
- Hydrolyzes terminal sialic acid residues from glycoproteins and glycolipids, influencing cell–pathogen interactions.
- Valuable in glycobiology for studying the role of sialic acid in host–pathogen recognition.
The Sigma-Aldrich Neuraminidase from Vibrio cholerae, Type III is a purified, reliable enzyme reagent for research in glycobiology, pathogen-host interaction studies, diagnostic assay development, and substrate specificity research. With high activity and consistency, this preparation is widely trusted in academic, clinical, and pharmaceutical laboratories.
- Pack Size: 1 UNIT 2 UNITS