GlycOCATCH Affinity Purification


GlycOCATCH purifies and enriches mucin-type O-glycosylated proteins and peptides



GlycOCATCH contains spin columns with inactive OpeRATOR (OgpA) enzyme immobilized on agarose beads. The immobilized inactive enzyme specifically binds core 1 O-glycans for enrichment and purification of mucin-type O-glycosylated proteins and peptides. GlycOCATCH performance is optimal after desialylation using SialEXO and captured O-glycoproteins can be eluted using 8 M urea or active OpeRATOR enzyme. GlycOCATCH is available in spin columns for affinity-capture of 200 ug of O-glycoprotein and supplied with lyophilized SialEXO for preparative desialylation and OpeRATOR enzyme for elution.

Detailed Information


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Digestion Site



Reaction Conditions

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Buffer Compatibility

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Unit Definition


Yes. IMPORTANT! Before you load your sample make sure that the protease in solution is inactivated and that the pH, buffer, chaotrope and NaCl concentrations are within the recommended ranges according to the instructions.

No, GlycOCATCH is designed to bind specifically to mucin type (core 1) O-glycosylated proteins and peptides. The performance is significantly enhanced by removal of sialic acids using SialEXO.

No, when the glycoprotein is digested with OpeRATOR, the binding capacity of GlycOCATCH is lost.

The OpeRATOR enzyme digests O-glycosylated proteins N-terminally to the serine (S) and threonine (T) glycosylation sites. OpeRATOR therefore facilitates mapping of O-glycosylation sites by LC-MS and as the digested products no longer bind to the GlycOCATCH resin, elution and sample preparation can be achieved in a single step. However, this requires the O-glycosylation sites to be spaced closely together for the OpeRATOR digestion to yield peptides of a size suitable for analysis by LC-MS/MS.

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