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α(2-3,6) Sialidase Cp cleaves all non-reducing terminal non-branchedα(2-3) andα(2-6) sialic acid residues from complex carbohydrates and glycoproteins. There is no detectable activity onα(2-8) orα(2-9) linkages or on branchedα(2-3) orα(2-6) linkages. The relative cleavage rates for different linkages are:α(2-3) >α(2-6). α(2-3,6) Sialidase Cp will not cleave branched sialic acids (linked to an internal residue). Useα(2-3,6,8,9) Sialidase Au (E-S001) forα(2-8) or branched sialic acids. To cleave only non-reducing terminalα(2-3) unbranched sialic acid residues, useα(2-3) Sialidase Sp (E-S007). α(2-3,6) Sialidase Cp is isolated from a clone ofClostridium perfringens. The enzyme has been extensively characterized using oligosaccharide standards.
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1,2-O-Isopropylidene-β-L-idofuranuronic-6-13C acid γ-lactone
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1,2-O-Isopropylidene-β-L-idofuranuronic-1,6-13C2 acid γ-lactone
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1,2,3,6-Tetra-O-benzoyl-β-D-mannopyranose
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2,3,4,6-Tetra-O-acetyl-β-D-glucopyranosyl fluoride
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2-O-(2-Acetamido-2-deoxy-β-D-galactopyranosyl)-D-galactose
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Lactosylceramid
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4-Methylphenyl 4,6-O-benzylidene-1-thio-β-D-galactopyranoside
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4-Methylphenyl 2,3-di-O-benzyl-4,6-O-benzylidene-1-thio-α-D-mannopyranoside