GalNAcEXO®
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GalNAcEXO is an α-N-Acetylgalactosaminidase for efficient hydrolysis of terminal GalNAc residues on glycoproteins.

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GalNAcs linked to serine or threonine, referred to as Tn antigen, are quickly and efficiently hydrolyzed by GalNAcEXO, and the enzyme also displays activity on α1-3-linked terminal GalNAcs.
The enzyme is a valuable tool that reduces sample heterogeneity for the analysis of complex O-glycoproteins that carry α-linked GalNAc residues as immature truncated core 1.
α-linked GalNAc residues on O-glycoproteins
4 h reaction
No need for co-factors
Tn antigen and α1-3-linked terminal GalNAc
Lyophilized enzyme for hydrolysis of GalNAc residues on glycoproteins
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Immobilized enzyme for hydrolysis of GalNAc residues on glycoproteins in spin columns
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GalNAcEXO is an exo-α-N-Acetylgalactosaminidase for efficient hydrolysis of α-N-Acetylgalactosamine (GalNAc) linked to serine or threonine residues in glycoproteins (Tn antigen). The enzyme also displays activity on α1-3-linked terminal GalNAc.
GalNAcEXO hydrolyzes GalNAc on glycoproteins under native conditions and is highly active in the pH range 6.0 to 7.6. No co-factors or special buffers are required. The enzyme in GalNAcEXO is derived from Akkermansia muciniphila, expressed in E. coli with a His-tag, and has a molecular weight of 52 kDa.
Confirmation and quantification of Tn antigens on O-glycosylated biopharmaceuticals while simplifying intact-mass analysis and revealing protein variants.
O-glycan site occupancy profiling and complete deglycosylation of etanercept for in-depth characterization of complex O-glycoproteins.
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