Welcome to our blog! This is where we share a bit more – insights, updates, and thoughts from Genovis. Take a look around and see what you find.
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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!
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…
At the annual ASMS meeting, we proudly showcase the latest SmartEnzymes™ applications! Many of our customers will also present posters and oral presentations, highlighting how SmartEnzymes have enhanced their specific projects. This digested guide to ASMS features the most anticipated posters and presentations that we’re excited about. We hope it inspires you and helps you…
We are thrilled to announce the speaker for our next GenovisWebinar! We are happy to welcome Sarah Smith from Immunocore to talk about her experiences using SmartEnzymes™. Please join us to learn about how Sarah and her team have used GlySERIAS™ to optimize their analytical workflows for enhanced identification and quantification of the oxidation…
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…
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.
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…
Scientists at Université de Bourgogne and collaborators have described the development of a bimodal tracer targeting PD-L1 in human and murine models for preclinical studies. Using a [111In]-DOTA-aza-BODIPY bimodal probe following conjugation onto PD-L1 monoclonal antibodies (mAbs) through either site-specific or random methods, the ability of the bimodal antibodies to selectively identify PD-L1+ tumors were…
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…
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…
We are excited to announce the speaker and topic for our next GenovisWebinar!
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.
