Articles in the Category ”News”
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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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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NEW! We’re Launching IgASAP™ for Digestion of IgA!
IgASAP Sub1 is an IgA1-specific protease that digests human IgA1 at one specific site above the hinge, generating intact and homogeneous Fab and Fc fragments.
The enzyme enables 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 ImpaRATOR™!
We are excited to launch ImpaRATOR, an O-glycan-dependent protease that digests proteins carrying mucin-type O-glycans, including sialylated species, N-terminally of glycosylated Ser and Thr residues!
The enzyme generates glycopeptides carrying O-glycans, which enables O-glycan profiling, site occupancy determination and O-glycopeptide mapping as well as middle-level approaches using LC-MS analysis.
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NEW! We’re Launching IgMBRAZOR™!
IgMBRAZOR is a unique IgM-specific protease that digests human IgM at one specific site below the CH2 domain in the heavy chain, generating homogeneous F(ab’)2 and Fc fragments. We’re excited to launch this unique tool today that enables middle-level analysis of the complex and high molecular weight human IgM!
IgMBRAZOR facilitates IgM characterization during, for example, the development of vaccines, therapeutics, and diagnostics. The digestion is complete within 30 minutes, and due to the specificity of the enzyme, there is no risk of overdigestion if the incubation time is prolonged.
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Collaboration Agreement
Genovis and ArcticZymes are excited to announce a collaboration to speed up penetration and growth in the Chinese market.
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