SialEXO 23 contains a sialidase acting specifically on α2-3 linked sialic acids. The SialEXO 23 enzyme hydrolyzes all α2-3 sialic acids from N- and O-glycosylated proteins and peptides as well as released glycans. SialEXO23 is available as lyophilized powder for α2-3-specific desialylation of 0.5 mg of sialylated glycoproteins.
| Application | |
|---|---|
| Product Group | |
| Source/Origin | Cloned from A. muciniphila, Produced in E. coli (His-tagged), 66 kDa |
| Product Composition | |
| Digestion Site | |
| Specificity | |
| Substrates | |
| Reaction Conditions | 1-2 hour reaction at 37°C according to protocol specifications |
| Digestion Buffers | |
| Buffer Compatibility | Other buffers or pH (7.0 – 9.0) can be used but the reaction conditions need to be optimized. |
| Inhibitors | |
| Unit Definition | 1 unit hydrolyzes ≥ 90% a2-3 sialic acids of 1 µg glycoprotein (fetuin) |
Yes, SialEXO displays activity on sialic acids with α2-3, α2-6 and α2-8 linked bonds of both N- and O-glycans.
Yes, SialEXO can be incubated together with OpeRATOR and/or OglyZOR in 20 mM Tris pH 6.8.
Yes, both enzymes are active under native conditions, preferably use 20 mM Tris pH 7. If denaturing reaction conditions are required for PNGaseF, the reaction with SialEXO needs to be performed first under native conditions, then add PNGaseF and the required buffer.
Yes, you can. All three enzymes perform well in the same reaction buffer (20 mM Tris pH 6.8). There is no need to increase incubation time when combining the enzymes.
Yes, SialEXO contains a 6x His-tag.
No, SialEXO works both on glycoproteins in native conditions but can also be used on denatured proteins after buffer exchange.
