GlyCLICK® Enhances Development of Immuno-SPECT/Fluorescent Tracer for PD-L1 in Preclinical Models


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 assessed using both fluorescence and SPECT imaging. There were significant benefits observed with the probe generated using the GlyCLICK site-specific conjugation method compared to a random lysine conjugation approach!
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NEW! We’re Launching PNGase F Automation!

January 31, 2024 | New Product, News |

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!

December 10, 2023 | New Product, News, Products |

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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Sign up for our next GenovisWebinar!

October 6, 2023 | GenovisWebinars |

We are excited to announce the speaker and topic for our next GenovisWebinar!

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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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IP Rights to Novel Enzymes for Applications within Genomics

April 25, 2023 | News, Press Releases |

Today, Genovis has acquired the patent rights to a unique DNA polymerase developed by researchers at Uppsala University. The enzyme has potential applications in research, diagnostics and forensics.
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Sign Up for our Next GenovisWebinar!

April 21, 2023 | GenovisWebinars |

We are excited to announce the speaker and topic for our next GenovisWebinar!
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Mechanistic Insights to Drive Rational Design of Masked Antibodies using FabALACTICA®


Scientists at the University of Cambridge, Astra Zeneca and collaborators undertook mechanistic studies to investigate antibody masking and better understand the parameters involved and their relative impact. FabALACTICA proved to be a valuable tool in this study, allowing the authors to generate antibody subunits. Using the Fab region, as opposed to the full-length antibody, allowed for both higher resolution SEC-MALS experiments to be performed, and supported structural determination of the complexes.
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