|form||buffered aqueous solution|
|25 units/100 μL protein|
|ml wt||Mᵣ = 27 kDa|
|packaging||300 μL liquid |
|optimum pH||5.0 - 5.5|
|shipped in||sent cooled at 4°C|
Endoglycosidase H cleaves between the N-acetylglucosamine residues of the chitobiose core of N-linked glycans, leaving one N-acetylglucosamine residue attached to the asparagine. The specificity of this enzyme is such that oligomannose and most hybrid types of glycans, including those that have a fucose residue attached to the core structure, are cleaved whereas complex type glycans are not released. Thus, this enzyme is extremely useful for selective release of high mannose (oligomannose) or hybrid type glycans from glycoproteins. The enzyme is also active against dolichol-linked glycans containing these structures.
For life science research only. Not for use in diagnostic procedures.
Enzyme/substrate ratio should be in the range of 0.04 U/25-80 μg.
Cleaves between the two N-acetylglucosamine residues in the N-linked diacetylchitobiose glycan core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine.
300 μL enzyme solution.
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