GalNAcEXO® – Hydrolysis of α-linked GalNAcs

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

SmartEnzymes™

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.

Why GalNAcEXO®?

  • Highly efficient α-N-Acetylgalactosaminidase – fast and complete removal of Tn-antigen and α1-3-linked GalNAc
  • Enables complete glycan removal for improved protein characterization
  • Available immobilized in ready-to-use spin columns
  • Target

    α-linked GalNAc residues on O-glycoproteins

  • Time

    4 h reaction

  • Box

    No need for co-factors

  • Digestion Site

    Tn antigen and α1-3-linked terminal GalNAc

Product Formats

About GalNAcEXO®

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.

Applications

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FAQ and Support

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