OglyZOR™ Requires Removal of Sialic Acids

Performance Activity

Hydrolyzes core 1 O-glycans from native glycoproteins, supporting LC-MS workflows for accurate PTM mapping and protein characterization.

The OglyZOR enzyme efficiently hydrolyzes core 1 disaccharides (Gal-β1,3-GalNAc) from native glycoproteins. This makes the enzymes suitable for preparation of samples prior to LC-MS analysis for identification of other PTMs or confirmation of amino acid sequences. 

To investigate the OglyZOR activity on native glycoproteins, the enzyme was incubated with etanercept, TNFR and abatacept for 1 h at 37°C with or without SialEXO. When the sialic acids are removed, the OglyZOR enzyme efficiently hydrolyzes the O-glycans from all three substrates.

SialEXO is required for efficient core-1 O-glycan hydrolysis

Efficient O-glycan removal from native glycoproteins using OglyZOR and SialEXO. O-glycosylated substrates; etanercept, TNFR and abatacept, were incubated with OglyZOR, with or without SialEXO, for 1 hour at 37 °C and analyzed by SDS-PAGE.

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