OglyZOR is an O-glycosidase that specifically hydrolyzes core 1 mucin-type O-glycans on proteins and peptides. The OglyZOR enzyme is active on native (non-denatured) substrates and the performance is optimal after desialylation using SialEXO. OglyZOR is available as lyophilized powder for deglycosylation of 2 mg of O-glycoprotein and supplied with lyophilized SialEXO for preparative desialylation.
| Application | |
|---|---|
| Product Group | |
| Source/Origin | Cloned from S. oralis, Produced in E. coli (His-tagged), 227 kDa |
| Product Composition | Lyophilized in TBS, Purified to ≥ 90% homogeneity, SialEXO included |
| Digestion Site | |
| Specificity | |
| Substrates | |
| Reaction Conditions | 2-4 hour reaction at 37°C according to protocol specifications |
| Digestion Buffers | |
| Buffer Compatibility | Other buffers or pH (6.5 – 7.5) can be used but the reaction conditions need to be optimized. |
| Inhibitors | |
| Unit Definition | 1 unit removes ≥ 90% O-glycans of 1 µg glycoprotein (TNFaR) in combination with 1 unit SialEXO |
Yes, we have performed successful experiments with OglyZOR, SialEXO and PNGaseF in the same reaction under native conditions O/N at pH ~7.0. If denaturing reaction conditions are required for PNGaseF, the reaction with OglyZOR and SialEXO needs to be performed first under native conditions, then add PNGaseF and the required buffer.
Yes, this workflow enables MS/MS of O-glycosylated peptides with removed O-glycans.
OglyZOR only works on desialylated O-glycans therefore is a sialidase (SialEXO) included with the product. SialEXO is not O-glycan specific and will therefore desialylate any N-glycans that are present.
No, OglyZOR recognizes the core 1 disaccharide HexNAcHex (or GalNAcGal) and to some extend also the core 3 disaccharide HexNAc(2) (or GalNAcGlcNAc).
