ImpaRATOR™
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ImpaRATOR™ Lyophilized
Lyophilized enzyme for digestion of mucin-type O-glycoproteins and peptides, including sialylated O-glycan species
ImpaRATOR is an O-glycan-dependent protease that digests proteins carrying mucin-type O-glycans, including sialylated species, N-terminally of glycosylated Ser and Thr residues.
ImpaRATOR Lyophilized is available as a lyophilized powder in 2000 unit vials for digestion of 2 mg O-glycosylated protein.
Why ImpaRATOR™ Lyophilized?
- Flexible format for method development
- Possible to combine enzymes for improved efficiency
- Amenable to automated workflows
- Ready to use – just add water!
Available Products
ImpaRATOR™ Lyophilized 2000 units
Lyophilized enzyme for digestion of 2 mg mucin-type O-glycoproteins and peptides, including sialylated O-glycan species
For information on how to order, visit Place an Order or contact us directly at order@genovis.com.
Product Information
Unit Defintion
One unit ImpaRATOR Lyophilized digests ≥ 95% of 30 µg etanercept at least at one site when incubated in TBS (50 mM Tris-HCl, 150 mM NaCl), pH 7.6 at 37°C for 30 minutes. For O-glycopeptide mapping applications, one unit ImpaRATOR Lyophilized digests 1 µg O-glycosylated protein when incubated in TBS, pH 7.6 at 37°C for 2 hours.
Content and Storage
ImpaRATOR Lyophilized is supplied lyophilized in TBS (50 mM Tris-HCl, 150 mM NaCl), pH 7.6, with no preservatives added.
ImpaRATOR Lyophilized is shipped at ambient temperature, and should be stored at -20°C upon arrival.
After reconstitution, the ImpaRATOR enzyme is stable for at least 1 month at +4-8°C.
Resources
Instruction for Use
Product Specifications
Safety Data Sheet
Certificate of Analysis
Find your certificate of analysis »SmartEnzymes™ for the Glycosylation Charcterization of Glycoproteins
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Applications
Combining multiple digestions for O-glycan site mapping with glycan structure analysis for complete characterization of heavily O-glycosylated proteins.
Broad O-glycan substrate acceptance efficiently generating informative O-glycopeptides while retaining glycan structure information.
FAQ and Support
Are there any known inhibitors of ImpaRATOR?
ImpaRATOR is a metalloprotease and thereby sensitive to chelating agents such as EDTA. Concentrations > 1 mM EDTA results in complete inhibition of the enzyme. In addition, the ImpaRATOR activity is inhibited by reducing agents and detergents.
Does ImpaRATOR cleave at all O-glycosylated sites?
ImpaRATOR has a broad activity towards different O-glycan structures; however, the enzyme has limited activity towards sites with two adjacent O-glycosylated Ser/Thr residues. For complete information about O-glycan sites in glycoprotein substrates containing several sites with two adjacent O-glycosylated Ser/Thr residues, OpeRATOR may be a better option.
Can ImpaRATOR be used under denaturing conditions?
Insufficient digestion during non-denaturing conditions can be caused by O-glycosylation sites within the glycoprotein inaccessible to the enzyme. In such cases, we recommend trying the following workflow: reduction, denaturation, carboxymethylation, buffer-exchange, and then digestion with ImpaRATOR. If detergent is added, make sure to include a detergent removal step prior ImpaRATOR digestion.
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