SialEXO™
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Lyophilized enzyme for hydrolysis of ɑ2-3-linked sialic acids

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 2-3 Lyophilized is available as a lyophilized powder in 500 unit vials for desialylation of 0.5 mg glycoprotein.
In contrast to SialEXO, which is a sialidase mix, SialEXO 2-3 is an α2-3 specific sialidase, allowing targeted analysis of α2-3 linked sialic acids only. Efficient α2-3 desialylation of O- and N-glycosylated proteins can be achieved within 1 h.
SialEXO 2-3 hydrolyzes glycoproteins under native conditions and displays activity in pH ranging from 7.0 to 9.0. The enzyme is derived from Akkermansia muciniphila and expressed in E. coli. The enzyme has a His-tag and the molecular weight is 66 kDa.
Lyophilized enzyme for hydrolysis of ɑ2-3-linked sialic acids from 0.5 mg glycoprotein

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One unit of SialEXO 2-3 Lyophilized hydrolyzes α2-3 linked sialic acids from ≥ 90% of 1 µg glycoprotein (fetuin) when incubated in 20 mM Tris pH 7.5 at 37 °C for 1 h.
SialEXO 2-3 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.
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.
Yes, SialEXO can be incubated together with OpeRATOR and/or OglyZOR in 20 mM Tris pH 6.8.
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.
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