Sialidase Cp α(2-3,6) [For Glycan Release] (CAT#: CB-P263-K) Datasheet

Kit

Α(2-3,6) sialidase Cp cleaves all non-reducing terminal and non-branched α(2-3) and α(2-6) sialic acid residues in complex carbohydrates and glycoproteins. For α (2-8) or α(2-9) linkage or branched α(2-3) or α(2-6) linkage. The relative cleavage rate of different linkages is: α(2-3)>α(2- 6).
Α(2-3,6) sialidase Cp was isolated from the clone of Clostridium perfringens. The enzyme has been extensively characterized using oligosaccharide standards.

Source: Recombinant from Clostridium perfringens in E. coli.

EC: 3.2.1.18

Alternate Names: Neuraminidase, NANase, N-acetylneuraminate glycohydrolase, Exo-α-sialidase

Specific Activity:>250 U/mg
Activity:>15 U/mL

Molecular weight: 41,000 daltons

pH range: 50 mM sodium phosphate (pH 6.0) provides the optimal buffer for enzyme activity with 3'-siayllactose, a standard substrate. If glycosidase treatment is performed at suboptimal pH because of glycoprotein solubility or activity requirements, expect some diminution in enzyme activity.

Specificity: Cleaves all nonreducing terminal non-branched α(2-3) and α(2-6) sialic acid residues from complex carbohydrates and glycoproteins.

Specific Activity Assay: Defined as the amount of enzyme required to produce 1 µmole of methylumbelliferone in 1 minute at 37°C, pH 5.0 from MU-NANA [2'-(4-methylumbelliferyl)-α-D-N-acetylneuraminic acid].

Sialidase Cp cleaves all non-reducing terminal non-branched α(2-3) and α(2-6) sialic acid residues from complex carbohydrates and glycoproteins.