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Endo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It also will cleave high mannose glycans but at a 40x reduced rate. It cleaves between the two N-acetylglucosamine residues in the diacetyl chitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Endoglycosidase F2 is less sensitive to protein conformation than PNGase F and is, therefore, more suitable for deglycosylation of native proteins. However, for optimal results, denaturation of the glycoprotein is recommended. Recombinant gene from Elizabethkingia miricola in E. Coli Kit includes enzyme plus reaction buffer. Sufficient for up to 60 reactions.
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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