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Sigma Aldrich, Neuraminidase from Vibrio cholerae, 1 UNIT
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Type II, buffered aqueous solution, 8-24 units/mg protein (Lowry, using NAN-lactose)
Specifications:
| Application | Protein Biology, cell Signalling | ||
| Storage Temperature | 2-8°C | ||
| Product Type | Proteins & Peptides | Forms | Liquid |
| Product Brand | Sigma-Aldrich | ||
| Product Grade | Molecular Biology | ||
Sialic Acid–Cleaving Enzyme for Glycoconjugate and Cell-Surface Studies
This Type II neuraminidase from Vibrio cholerae is supplied as a buffered aqueous solution with a specific activity of 8–24 units/mg protein, determined using the Lowry method with NAN-lactose as substrate. Neuraminidases (sialidases) hydrolyze terminal sialic acid (N-acetylneuraminic acid) residues from glycoconjugates and are widely used in glycobiology, virology, and cell-surface receptor studies.
In V. cholerae, this enzyme contains lectin-like domains flanking its catalytic center, enhancing substrate recognition and binding to complex sialylated molecules. This preparation contains protease and NAN-aldolase activity, and is preservative-free for sensitive biochemical applications.
Product Specifications
| Property | Value |
|---|---|
| Product Name | Neuraminidase from Vibrio cholerae (Type II) |
| CAS Number | 9001-67-6 |
| EC Number | 3.2.1.18 / 232-624-6 |
| MDL Number | MFCD00131711 |
| Source Organism | Vibrio cholerae |
| Form | Buffered aqueous solution |
| Type | Type II |
| Specific Activity | 8–24 units/mg protein (Lowry, NAN-lactose) |
| Physical Form | In 50 mM sodium acetate (pH 5.5), 0.15 M NaCl, 4 mM CaCl₂; 0.2 µm filtered |
| Storage Temperature | 2–8 °C |
| Preservatives | None |
| Foreign Enzyme Activities | Protease and NAN-aldolase, present |
| Pack Size | 1 unit (SKU: N6514-1UN) |
Unit Definition
One unit will release 1.0 µmol of N-acetylneuraminic acid per minute at pH 5.0 and 37 °C using NAN-lactose or bovine submaxillary mucin as substrate.
Applications
- Hydrolysis of terminal sialic acids in glycoconjugates
- Probe for glycan structure and distribution on cell surfaces
- Substrate specificity and lectin domain binding studies
- Modification of tumor or immune cell surfaces for functional analysis
- Used in virus research, including mechanisms of influenza and pathogen dissemination
- Preparative glycan trimming for LC-MS or immunological analysis
Supporting Literature
- Lectin domains assist substrate recognition: [Calorimetry Studies]
- Five-step purification of Vibrio neuraminidase: (J. Biochem., [1999])
- Leukemia cell surface modification study: (Tumor Immunol., [1988])
Sigma-Aldrich Neuraminidase from Vibrio cholerae, Type II is a versatile sialidase suitable for glycoprotein research, cell-surface mapping, and glycoconjugate modification. With moderate specific activity and broad substrate recognition via lectin-like domains, this enzyme is ideal for functional studies in glycobiology, virology, and immunology. It provides a reliable tool for researchers investigating sialylation-dependent cell signaling, virus-host interactions, or glycoprotein structure-function relationships.