Welcome to Join Our First GenovisWebinar!
We are excited to announce our series of GenovisWebinars, and we are happy to invite you to the first webinar held on November 17th!
Each webinar will showcase inspirational SmartEnzymes user, and the topics discussed are influenced by how to improve analytical workflows. Please join us in sharing experiences!
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Localization of O-glycan Sites in CD24Fc by OpeRATOR® Digestion and LC-MS Analysis
Scientists from Merck & Co. and Glycotope describe the localization of 12 O-glycosylation sites in the heavily O-glycosylated fusion protein CD24Fc by digestion with the O-glycoprotease OpeRATOR in combination with LC-MS analysis. Two different workflows were developed, one based on fractionation in combination with LC-MS/MS CID and one based on LC-MS/MS EThcD. OpeRATOR digestion enabled the localization of O-glycan sites in both workflows and relative quantification of different glycoforms.
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Antibody LC-MS Analysis Service from Genovis!
We offer fast and accurate LC-MS profiling of human IgG using unique sample preparation based on SmartEnzymes workflows. Our SmartEnzymes enable middle-level LC-MS analysis of antibodies to characterize critical quality attributes such as the glycosylation profile and mass confirmation.
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FabRICATOR® in Correlative N-glycan Analysis of Cetuximab Produced in Different Expression Systems
A strategy for comparative characterization of cetuximab produced in a variety of expression cell lines is described in this paper from scientists at the National Institute for Bioprocessing Research and Training (NIBRT) in Dublin, Ireland. FabRICATOR (IdeS) is a critical tool in this study, allowing for site-specific glycan analysis to be performed following antibody digestion into F(ab’)2 and Fc/2 subunits.
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The Click Chemistry used in GlyCLICK® is Awarded the Nobel Prize!
Every autumn, the Royal Swedish Academy of Sciences announces the winners of the prestigious Nobel Prize. This year’s Chemistry Prize goes to Carolyn Bertozzi, Barry Sharpless and Morten Meldal for the development of click chemistry and bioorthogonal chemistry. Click chemistry is a fundamental part of our GlyCLICK technology. By combining Fc glycan remodeling and the award-winning click chemistry, GlyCLICK enables site-specific labeling of antibodies!
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Unravelling Structural Conformers within a Therapeutic Multispecific mAb using FabALACTICA
Scientists at the University of Strasbourg and Sanofi describe the global structural characterisation of a trispecific antibody which exhibits two distinct structural isoforms when analyzed by size-exclusion chromatography (SEC). FabALACTICA proved to be a valuable tool in this study as above hinge digestion of this trispecific antibody allowed for middle-level characterisation of the isomeric Fab regions and facilitated cyclic-ion mobility (cIM) differentiation of the isomers, which was not possible in the intact molecule without prior SEC separation.
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FabRICATOR® in Middle-Up Quantitative N-Glycan Profiling of Therapeutic Monoclonal Antibodies
A middle-level approach to glycan characterisation is described in this paper by scientists at the University of Geneva and collaborators. FabRICATOR (IdeS), a critical tool in this study, is used to generate Fd’, LC and the glycan-containing Fc subunits, which can be chromatographically separated using HILIC and characterised using mass spectrometry.
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Genovis Enters Licensing and Supply Agreement with New Bioprocess Customer
We have signed a long-term licensing and supply agreement with a new bioprocess customer!
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LC-MS Analysis Service of Recombinant Antibodies
We have entered a service agreement with evitria AG (Zürich, Switzerland) to offer a fast and high-quality LC-MS characterization of recombinant antibodies using our SmartEnzymes™ workflows!
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NEW! Hydrolysis of Flexible Linkers using GlySERIAS
GlySERIAS is a unique enzyme that digests flexible glycine-rich fusion protein linkers such as Gly4Ser and GlyxSery (GS) and polyglycine (G) linkers.
The enzyme enables separation of the individual domains of multi-functional fusion proteins to facilitate characterization and increase the understanding of these molecules. Middle-level analysis of fusion proteins serves to both reduce the overall sample complexity and allow for domain-specific identification and monitoring of post-translational modifications.
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