Articles in the Category ”News”

SmartEnzymes™ for Gene Therapy

May 11, 2022 | News, Products |

The development of advanced gene therapies is promising and gives thousands of patients new hope for a curative treatment. However, many of the current gene therapies are using adeno-associated viruses as transporters of new genetic material. Up to 60% of patients may have antibodies against this viral vehicle and this is usually an exclusion criteria for being eligible for gene therapy. To overcome the presence of neutralizing antibodies, a new strategy includes the use of highly specific IgG proteases to digest the antibody population and increase the uptake of the new genetic material.
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NEW! Azide Activation of Human IgG using TransGLYCIT Azide Activation

April 4, 2022 | New Product, News |

We’re happy and proud to announce the launch of TransGLYCIT Azide Activation!
 
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NEW! PNGase F for Hydrolysis of N-glycans

November 29, 2021 | New Product, News |

We are happy to announce that PNGase F for in-solution hydrolysis of N-glycans from glycoproteins is added to our portfolio of SmartEnzymes!
 
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NEW FabDELLO – The SmartEnzyme for Mutated IgG

November 18, 2021 | New Product, News |

We introduce FabDELLO, a protease that specifically digests human IgG1 at a single site above the hinge, generating intact Fab and Fc fragments within two hours with no need for reducing conditions. The enzyme is active on antibodies with mutated hinge regions and enables middle-level LC-MS for characterization of critical quality attributes.
 
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NEW SmartEnzyme – Immobilized PNGase F for Fast N-glycan Hydrolysis!

October 10, 2021 | New Product, News |

Genovis launches Immobilized PNGase F, a resin with the PNGase F enzyme covalently coupled to agarose beads for hydrolysis of N-glycans on antibodies, fusion proteins and other N-glycosylated proteins in a convenient spin column format. 

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NEW TransGLYCIT™ Glycoforms Available!


Genovis launches new glycoforms with TransGLYCIT™ – A platform to create IgG with defined glycan profiles!

 

TransGLYCIT enables specific IgG N-glycan remodeling and prepares antibodies with a defined and homogenous G0, G1, G2 or G2S2 glycoform using fast and robust enzymatic workflows. With the optional FucosEXO™ 16 enzyme, afucosylated antibodies can be obtained that enable direct comparison of antibodies with or without the core fucose.

 

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New Application Note on Antibody Oxidation Analysis


A Rapid LC-MS Assay for Monitoring of mAb Oxidation at the Subunit Level
 
Methionine oxidation is considered a critical quality attribute of therapeutic antibodies and may impact the clinical safety and efficacy. Therefore, monitoring of methionine oxidations is required during the discovery, development, and production of therapeutic antibodies. Traditional methods to characterize oxidation rely on tryptic peptide mapping and LC-MS, a labor intensive and time- consuming process that generates large data sets and requires trained and skilled manual interpretations.
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Launching New Anti-FabRICATOR Formats!

May 7, 2021 | New Product, News |

We are happy to announce two new affinity purified antibody formats for detecting the FabRICATOR enzyme!
 
The Anti-FabRICATOR Affinity Purified is an affinity purified goat polyclonal antibody and
the Anti-FabRICATOR Affinity Purified Biotin Conjugated is an affinity purified and biotin-conjugated goat polyclonal antibody.
 
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Characterization of SARS-CoV-2 Receptor-Binding Domains using SmartEnzymes™


Scientists at Leiden University Medical Center (LUMC) present a multilevel mass spectrometry approach using SmartEnzymes for in-depth characterization of mammalian SARS-CoV-2 receptor-binding (RBD) domains.

 

The COVID-19 disease caused by the SARS-CoV-2 virus has affected more that 100 million individuals in the ongoing pandemic. The enveloped RNA corona virus contains three structural proteins in the membrane, including the heavily glycosylated spike protein carrying 22 N-glycosylation sites. The spike protein in turn consists of two subunits, S1 and S2, where the receptor-binding domain (RBD) of S1 directly interacts with the ACE2 receptor in the human respiratory tract and facilitates host cell entry. Considering the relevance of RBD glycosylation on ACE2 binding and recognition by neutralizing antibodies, the use of well-characterized S proteins is essential for continued research and development of diagnostic tools and vaccines.

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Genovis Teams up with Waters to Deliver Enzymatic Workflows for the Biopharma Industry


The new collaboration between Genovis and Waters Corporation is intended to bring fast and easy analytical workflows for biopharmaceuticals by combining the SmartEnzymes™ portfolio from Genovis with the unique instrumentation from Waters™. The lab work has already started, and we got a quick word with Andreas Nägeli, one of the scientists at Genovis contributing to this collaboration.

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