α2-3,6,8,9 Neuraminidase A
α2-3,6,8,9 Neuraminidase A is a broad specificity sialidase, which cleaves linear and branched non-reducing terminal sialic acid residues from glycoproteins, glycopeptides, and oligosaccharides. It can be used for glycan analysis and characterization and intact glycoprotein remodeling, in vitro and in vivo.
- Recombinant enzyme with no detectable endoglycosidase or other exoglycosidases contaminating activities
- Acts on both Neu5Ac and Neu5Gc
- Double digest with other exoglycosidases and endoglycosidases
- Tolerant of moderate levels (0.5-1.0%) of detergents
- ≥95% purity, as determined by SDS-PAGE and intact ESI-MS
- Optimal activity and stability for up to 24 months
Neuraminidase is the common name for Acetyl-neuraminyl hydrolase (Sialidase). α2-3,6,8,9 Neuraminidase A catalyzes the hydrolysis of all linear and branched non-reducing terminal sialic acid residues from glycoproteins and oligosaccharides. The enzyme releases α2-3 and α2-6 linkages at a slightly higher rate than α2-8 and α2-9 linkages.
α2-3,6,8,9 Neuraminidase A will cleave branched sialic acid residues that are linked to an internal residue. This oligosaccharide from fetuin is an example of a side-branch sialic acid residue that can efficiently be cleaved (1).
Product SourceCloned from Arthrobacter ureafaciens and expressed in E. coli (2).
The following reagents are supplied with this product:
Store at (°C) Concentration GlycoBuffer 1 -20 10 X
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