Evaluating the Impact of Antibody Fragments on Aggregation using FabALACTICA®
Scientists at Biogen have developed an approach to better understand monoclonal antibody (mAb) aggregation by characterizing fragments that may form during the production process. Fab/c fragments – common impurities generated through hinge digestion and loss of a Fab subunit – can offer valuable insights into aggregation mechanisms. To support this work, FabALACTICA, which specifically digests human IgG1 above the hinge, was used to generate structurally relevant Fab/c fragments. Its ability to produce consistent and defined mAb fragments makes FabALACTICA a powerful tool for studying mAb aggregation through this approach.
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Multi-Attribute mAb Variant Characterization with CE-MS and FabRICATOR® Digestion
Scientists at Aalen University and their collaborator present a detailed methodology for the rapid and thorough characterization of monoclonal antibody (mAb) variants using capillary electrophoresis-mass spectrometry (CE-MS) at the subunit level. mAbs are an important class of therapeutic molecules for treating various diseases, including cancer and autoimmune disorders. mAbs are large, complex molecules and can undergo a range of post-translational modifications (PTMs), which may affect their biological activity, stability, and therapeutic efficacy. Comprehensive characterization of these modifications is crucial to ensuring the safety and quality of therapeutic mAbs.
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GlyCLICK®-generated ADC Suppresses Tumor Growth in Pancreatic Cancer Models
Scientists at The Finsen Laboratory and collaborators have described the potential for a novel antibody-drug conjugate (ADC) to treat pancreatic ductal adenocarcinoma (PDAC). The ADC candidate is conjugated with a highly potent anthracycline payload (PNU-159682) using GlyCLICK conjugation technology, and targets uPAR (urokinase plasminogen activator receptor), a protein overexpressed in PDAC and its surrounding stroma. GlyCLICK facilitated the site-specific attachment of the payload to the antibody’s Fc-glycans, ensuring a precise drug-to-antibody ratio (DAR) of 2. This study highlights how GlyCLICK’s precision and efficiency significantly enhanced the development, efficacy, and safety of the ADC molecule.
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From Nobel Discoveries to New Frontiers in RNA Integrity
On this Nobel Day, we honor two monumental breakthroughs in RNA research recognized by the Nobel Prize in Physiology or Medicine! 🏆
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[GenovisWebinar!] 🤩 Unlocking Antibody Insights with Regeneron: SmartEnzymes™ in Action!
We are thrilled to welcome Xin Wang from Regeneron Pharmaceuticals to showcase how the reliability and robust performance of Genovis’ SmartEnzymes have enabled their subunit HILIC-MS method to be successfully applied across multiple Regeneron programs and commercial mAbs.
[New Launch] SEQURNA™ RNase Inhibitor Thermostable
We’re excited and proud to launch a new solution for securing RNA integrity!
SEQURNA RNase Inhibitor Thermostable is a fully synthetic and heat-tolerant inhibitor that protects RNA integrity. It is active across a wide temperature range, providing sustainability through ambient storage and shipping, minimizes batch effects, and avoids activity loss from freeze-thaw cycles and long incubation times. This makes it ideal for applications such as single-cell and in situ RNA sequencing, where preserving high-quality RNA is essential.
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SEQURNA™ Brings Synthetic RNase Inhibitors to Single-Cell Transcriptomics!
Scientists at the Karolinska Institute have demonstrated the construction of single-cell RNA sequencing (scRNA-seq) libraries using SEQURNA RNase Inhibitor Thermostable, a novel, fully synthetic, and thermostable RNase inhibitor. SEQURNA overcomes the limitations of traditional recombinant RNase inhibitors (RRIs) by providing superior thermal stability, enhanced reproducibility, and logistical convenience. Its use enabled the creation of high-quality single-cell libraries with increased experimental flexibility. The introduction of SEQURNA will significantly advance single-cell transcriptomics, making scRNA-seq more reliable and scalable!
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NEW! We’re Launching FabRICATOR Xtra LALA Lyophilized!
We’re excited to share that we are launching a new member of the SmartEnzymes™ family that will facilitate middle-level analysis of hinge-mutated IgG!
FabRICATOR Xtra LALA is an IgG-specific protease that digests antibodies which have been engineered to contain mutated hinges, including the LALA mutation. It digests below the hinge, generating F(ab’)2 and Fc fragments. FabRICATOR Xtra LALA is active on a variety of antibodies with mutated hinge regions and enables middle-level LC-MS characterization of critical quality attributes of hinge-mutated antibody-based therapeutics.
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Join Us for Our Next GenovisWebinar – Solve Analytical Challenges with SmartEnzymes™!
We are happy to welcome Angela Capolupo from Merck Serono to talk about how implementing Genovis SmartEnzymes in their workflows has allowed her and her team to resolve complex analytical and structural problems!
IgMBRAZOR™ in a Study on Structural Characterization of IgM
Scientists at Utrecht University and collaborators have described the use of online SEC combined with Orbitrap-based CDMS to perform real-time kinetic monitoring of pentameric IgM digestion by the protease IgMBRAZOR, a novel protease which digests specifically at a single site in the hinge region of IgM. While IgMBRAZOR was shown to efficiently digest IgM, it was observed that digestion of one of the F(ab’)2 subunits occurred more slowly than the other four. It is suggested that interactions of the J-chain within the pentameric IgM structure may influence the accessibility of the IgMBRAZOR enzyme, thus, impacting the digestion kinetics. SEC-CDMS allows the characterization of heterogeneous and large proteins, enabling unique experimental designs such as monitoring of reaction kinetics from physiological buffers.
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