Articles in the Category ”News”
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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[New 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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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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NEW! We’re Launching TransGLYCIT™ Remodeling Afucosylated Man5!
We are proudly launching a new format of our popular TransGLYCIT technology! With TransGLYCIT Remodeling Afucosylated Man5, it is possible to generate human IgG with fully homogenous Man5 glycoforms within a few hours!
TransGLYCIT is a platform technology that enables efficient and site-specific human IgG glycan remodeling or conjugation. With TransGLYCIT, antibodies with defined and homogenous glycoforms are generated using fast and robust enzymatic workflows.
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TransGLYCIT™ in a Study on Antibody Characterization
Scientists from the Wistar Institute in Philadelphia and collaborators have studied the IgG N-glycan structures and inflammatory aging markers of people living with and without HIV to determine a potential structure-function relationship. In this study, TransGLYCIT was used to generate anti-HIV antibodies with defined N-glycan structures to study Fc-mediated immune activities in vitro.
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Say Hello to IgASAP™ Sub1+2 Lyophilized!
IgASAP is a family of IgA-digesting enzymes. IgASAP Sub1 is an IgA1-specific enzyme that digests human IgA1 at one specific site above the hinge, and the enzyme we’re launching today, IgASAP Sub1+2, specifically digests IgA1 and IgA2m1 above the hinge. Both enzymes generate intact and homogenous Fab and Fc fragments.
The IgASAP enzymes enable generation of intact monovalent Fab fragments as well as middle-level analysis of IgA1, which facilitates IgA1 characterization during, for example, the development of vaccines, therapeutics, and diagnostics.
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NEW! We’re Launching PNGase F Automation!
PNGase F is a glycoamidase hydrolyzing the amide bond between the polypeptide asparagine and the innermost GlcNAc of all mammalian asparagine-linked complex, hybrid, or high mannose oligosaccharides. Today, we’re excited to launch this well-known enzyme in a new and unique format – PNGase F Automation – for automated hydrolysis of N-glycans on glycoproteins!
PNGase F Automation contains the PNGase F enzyme lyophilized in an automation-friendly 96-well plate format. It enables high-throughput N-glycan removal to facilitate simplified downstream analysis of a range of glycoprotein substrates.
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