SialEXO™
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The SialEXO products are sialidases for the removal and analysis of sialic acids. The enzymes are active on both N- and O-linked glycans present on native glycoproteins or released glycan structures.
SialEXO Lyophilized is available as a lyophilized powder in 2000 unit vials for desialylation of 2 mg glycoprotein.
Lyophilized enzyme mix for desialylation of 2 mg glycoprotein

For information on how to order, visit Place an Order or contact us directly at order@genovis.com.
One unit of SialEXO Lyophilized hydrolyzes sialic acids from ≥ 90% of 1 µg glycoprotein (fetuin) when incubated in 20 mM Tris pH 6.8 at 37 °C for 2 h.
SialEXO Lyophilized is reconstituted by addition of water. No preservatives added. After reconstitution, the enzyme is stable for 1 month at +4-8°C. The product is shipped at ambient temperature, and should be stored at -20°C upon arrival.
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Simplified charge variant analysis by removing sialic acid-driven heterogeneity to reveal underlying protein profile.
Complete desialylation of complex glycoproteins to simplify glycan profiles and enable more confident protein characterization.
Yes, SialEXO contains a 6x His-tag.
Yes, SialEXO can be incubated together with OpeRATOR and/or OglyZOR in 20 mM Tris pH 6.8.
No, SialEXO works both on glycoproteins in native conditions but can also be used on denatured proteins after buffer exchange.
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, SialEXO displays activity on sialic acids with α2-3, α2-6 and α2-8 linked bonds of both N- and O-glycans.
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