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The field of antibody-drug conjugates (ADCs) is rapidly emerging as a new, important class of cancer therapeutics. ADCs consist of monoclonal antibodies (mAbs) covalently linked to cytotoxic drugs, and after selective surface receptor binding on cancer cells, the drug is delivered into the intracellular compartment and can exert its cytotoxic effect.
We are happy to announce that PNGase F for in-solution hydrolysis of N-glycans from glycoproteins is added to our portfolio of SmartEnzymes!
We introduce FabDELLO, a protease that specifically digests human IgG1 at a single site above the hinge, generating intact Fab and Fc fragments within two hours with no need for reducing conditions. The enzyme is active on antibodies with mutated hinge regions and enables middle-level LC-MS for characterization of critical quality attributes.
Genovis launches Immobilized PNGase F, a resin with the PNGase F enzyme covalently coupled to agarose beads for hydrolysis of N-glycans on antibodies, fusion proteins and other N-glycosylated proteins in a convenient spin column format.
Our immune system protects us from pathogens and various diseases, and the immune response is dependent on a person’s repertoire of immune cells, antibodies and circulating plasma proteins. A detailed characterization of these plasma components is important for the understanding of how they affect each individual’s immune response.
In this paper, scientists at Spectroswiss and Orion Pharma present a novel strategy for DAR analysis of structurally complex antibody-oligonucleotide conjugates using SmartEnzymes™ and a proteoform integration approach combined with native SEC-Orbitrap FTMS.
Scientists at University of Geneva and Centre d’Immunologie Pierre-Fabre here describes a comprehensive intact and middle-level characterization of a commercial bispecific antibody by using a variety of orthogonal chromatographic methods coupled to MS.
Bottom-up mass spectrometry where the intact protein is digested into smaller peptides is an indispensable tool for proteomics and the studying of histone codes. Since histones are enriched with the basic amino acids arginine and lysine, enzymatic digestion is often challenging as peptides too short for LC retention and PTM localization are generated. In addition,…
Genovis launches new glycoforms with TransGLYCIT™ - A platform to create IgG with defined glycan profiles! TransGLYCIT enables specific IgG N-glycan remodeling and prepares antibodies with a defined and homogenous G0, G1, G2 or G2S2 glycoform using fast and robust enzymatic workflows. With the optional FucosEXO™ 16 enzyme, afucosylated antibodies can be obtained that enable…
The importance of monoclonal antibodies (mAbs) as therapeutic agents is steadily increasing, and each year nearly 300 novel mAbs are being evaluated for their therapeutic effectivity. Interest has also been expressed in the use of antibody fragments as therapeutic agents. The physiochemical properties of the fragments differ significantly from that of intact antibodies, and the…
Scientists at the University of Strasbourg and University of Geneva use innovative native MS and IM methodologies for analytical characterization of a site-specific ADC generated with the GlyCLICK technology. Antibody-drug conjugates (ADCs) combine the benefits of tumor-targeting monoclonal antibodies with the cytotoxic effect of drug payloads covalently linked to the antibody. The ADC generation…
With their molecular specificity for biological targets, monoclonal antibodies (mAbs) have revolutionized the field of research and medicine. Due to numerous post-translational modifications causing heterogeneity in the structure of mAbs, a comprehensive characterization of the physiochemical properties is necessary to ensure the quality, efficacy and safety of mAb-based therapeutic drugs.
