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Sigma-Aldrich, α2-3,6,8,9-Neuraminidase, Arthrobacter ureafaciens, Recombinant, E. coli, 250 mI.U.
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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 | ||
Broad-Specificity Sialidase for Glycoprotein and Glycan Analysis
This recombinant α2-3,6,8,9-neuraminidase (sialidase) is derived from Arthrobacter ureafaciens and expressed in E. coli. The enzyme cleaves non-reducing terminal sialic acid residues from glycoproteins and complex carbohydrates, targeting all major sialic acid linkages—α2-3, α2-6, α2-8, and α2-9. Its broad specificity makes it particularly valuable in glycoproteomics, structural glycomics, immunological research, and viral receptor studies.
This preparation is free of contaminating enzymatic activities including α/β-galactosidase, α/β-mannosidase, α-fucosidase, N-acetylglucosaminidase, and proteases, ensuring accurate and reproducible analytical results. It is supplied as a ready-to-use liquid in 20 mM Tris-HCl, 20 mM NaCl, pH 7.5, and is shipped on wet ice. The product remains stable at 2–8 °C and should not be frozen.
Product Specifications
| Property | Value |
|---|---|
| Source | Arthrobacter ureafaciens (recombinant, E. coli) |
| CAS Number | 9001-67-6 |
| EC Number | 3.2.1.18 |
| MDL Number | MFCD00040440 |
| Form | Liquid |
| Specific Activity | ≥40 U/mg protein; ≥5 U/mL |
| Buffer Composition | 20 mM Tris-HCl, 20 mM NaCl, pH 7.5 |
| Unit Definition | 1 unit = 1 µmol methylumbelliferone released/min at 37 °C, pH 5.0 |
| Storage Temperature | 2–8 °C (do not freeze) |
| Molecular Weight | Two active forms: ~60 kDa and ~69 kDa |
| Contaminant Activity | None detected (proteases, glycosidases) |
| Shipping | Wet ice |
| Pack Size | 250 mIU (SKU: 480716-250MIU) |
| Manufacturer / Brand | Sigma-Aldrich / Calbiochem® |
Applications
- Complete desialylation of glycoproteins, glycolipids, and glycoconjugates
- Glycan structure elucidation in mass spectrometry or HPLC workflows
- Immunology and receptor binding studies, including viral attachment analysis
- Biopharmaceutical quality control and glycosylation profiling
- Research on cellular recognition and signaling pathways
- Removal of terminal sialic acid residues to unmask underlying sugar epitopes
Key Features
- Broad substrate specificity for α2-3, α2-6, α2-8, and α2-9 sialic acid linkages
- No detectable contaminant enzyme activity (DNase, RNase, protease, etc.)
- Active in mild conditions (pH 5.0 at 37 °C)
- Liquid format, ready-to-use and stable at 2–8 °C
- High purity, recombinant source ensures batch consistency
- Compatible with biochemical assays, ELISAs, LC-MS, and Western blotting
Literature References
- Means, R.E. & Desrosiers, R.C. J. Virol. 2000, 74, 11181
- Prime, S. et al. J. Chromatogr. A 1996, 720, 263
- Roggentin, P. et al. Biol. Chem. Hoppe Seyler 1995, 376, 569
- Dwek, R.A. et al. Annu. Rev. Biochem. 1993, 62, 65
Safety Information
- Hazard classification: Harmful (C)
- Handle using appropriate PPE in a biosafety cabinet
- Refer to the Safety Data Sheet (SDS) for full hazard and handling information
Sigma-Aldrich α2-3,6,8,9-Neuraminidase is a high-performance, recombinant sialidase designed for broad-spectrum desialylation of glycoconjugates. Its specificity, stability, and contaminant-free profile make it a valuable tool for glycoprotein analysis, viral receptor studies, and biotherapeutic characterization. Whether you are conducting routine glycan trimming or complex glycomic mapping, this enzyme provides the reliability and reproducibility demanded by modern life science laboratories.