Endo S is an endoglycosidase specific for cleaving the N-linked glycans from the chitobiose core of the heavy chain of native IgG.
Active on native IgG
Tagged with a chitin binding domain (CBD) for easy removal
Recombinant enzyme with no detectable exooglycosidase or other endoglycosidases contaminating activities
Glycerol -free for optimal performance in HPLC and mass spectrometry analysis
≥95% purity, as determined by SDS-PAGE and intact ESI-MS
Optimal activity and stability for up to 12 months
Product Source
Endo S is cloned from Streptococcus pyogenes and overexpressed as a fusion to the chitin binding domain in E. coli.
Specificity
Detailed Specificity X = protein, peptide, Asparagine, or free glycan, as Endo S does not have a strict peptide requirement for activity. Endo S is active on a substrate with or without core α(1-6)fucosylation as well as a with or without a bisecting N-acetylglucosamine. Triantennary and tetrantennary sialyated or asialo glycans are not a substrate for Endo S.
Endo S is an endoglycosidase specific for cleaving the N-linked glycans from the chitobiose core of the heavy chain of native IgG.
Active on native IgG
Tagged with a chitin binding domain (CBD) for easy removal
Recombinant enzyme with no detectable exooglycosidase or other endoglycosidases contaminating activities
Glycerol -free for optimal performance in HPLC and mass spectrometry analysis
≥95% purity, as determined by SDS-PAGE and intact ESI-MS
Optimal activity and stability for up to 12 months
Product Source
Endo S is cloned from Streptococcus pyogenes and overexpressed as a fusion to the chitin binding domain in E. coli.
Specificity
Detailed Specificity X = protein, peptide, Asparagine, or free glycan, as Endo S does not have a strict peptide requirement for activity. Endo S is active on a substrate with or without core α(1-6)fucosylation as well as a with or without a bisecting N-acetylglucosamine. Triantennary and tetrantennary sialyated or asialo glycans are not a substrate for Endo S.