Articles in the Category ”News”

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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NEW SmartEnzymes – Launching FucosEXO!

Genovis launches FucosEXO, an α-fucosidase mix for efficient removal of α1-2, α1-3 and α1-4 linked Fucose on native N- and O-glycosylated proteins. 

 

Analysis of glycoproteins modified with complex glycan structures can be challenging and requires efficient and specific enzymatic tools. FucosEXO is a mix of α-fucosidases for efficient hydrolysis of α1-2, α1-3 and α1-4 linked fucose residues on N- and O-glycoproteins or oligosaccharides, without the need for co-factors or additives.

 

             

 

We have tested FucosEXO on a number of glycoengineered TNFR proteins carrying up to 11 O-glycans decorated with fucose in different linkages, comparing the activity to other commercially available fucosidases. FucosEXO is able to defucosylate the heavily glycosylated TNFR proteins within 1 hour, while treatment with other fucosidases only led to partial removal of fucose or no removal at all.

 

Learn more about FucosEXO for defucosylation of native glycoproteins.

 


 

 

 

FucosEXO enzyme – Lyophilized enzyme for removal of α1-2, α1-3 and α1-4 linked fucose from 2 mg glycoprotein.

 

Immobilized FucosEXO – Immobilized enzyme for removal of α1-2, α1-3 and α1-4 linked fucose from 0.5 mg glycoprotein.

 

 

 

Genovis receives funding from Vinnova

Genovis receives funding from Vinnova for the development of a new high-throughput platform for a directed and efficient product development for quality assurance of biological drugs. To understand the project we got a quick word with the VP of Research & Development at Genovis, Rolf Lood. Rolf is heading the enzyme discovery team at Genovis and has a solid scientific background from both Lund University and Rockefeller University, New York.

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SmartEnzymes in Targeted Sequencing of Heavily Glycosylated IgA1

The use of IgG-based antibodies in various clinical fields have increased over that past decades, continuing the development of better biopharmaceuticals. The use of other immunoglobulins including IgA, characterized with the ability to recruit effector cells, is progressively being considered a useful alternative. The complexity of the heavily glycosylated IgA does however pose analytical challenges and no method currently exist that allows unraveling of the human repertoire of this subclass.

 

Scientists at Utrecht University present a mass spectrometry method using electron capture dissociation (EDC) to obtain sequence ladders of the variable regions on the heavily N- and O-glycosylated anti-CD20 IgA1 antibody. Using SmartEnzymes and a native top-down approach, the scientists compared the IgA1 antibody to its anti-CD20 IgG counterpart, and their Fabs.

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Launching NEW GlyCLICK® ADC kits!

December 10, 2020 | Applications, News, Products |

Genovis launches new GlyCLICK kits for site-specific generation of custom ADCs carrying unique 2-step cleavable linker-payloads from Glykos Finland. 

 

Antibody-drug conjugates (ADCs) comprise a new generation of antibody-based biologics that carry drug payloads directly into target cells, allowing for a broadened therapeutic window. The drawbacks of conventional antibody conjugation strategies are rapidly being surpassed by site-specific methods, where conjugation at the Fc-glycan sites using GlyCLICK has proven to be an attractive option for labeling of native antibodies without genetic engineering.

 

The GlyCLICK conjugation technology results in site-specific incorporation of 2.0 drugs per antibody, for this reason the GlyCLICK ADC kits offer conjugation with highly potent payloads functionalized with DBCO to enable click-chemistry to azide activated antibodies. GlyCLICK ADC kits can be used to combine native IgG with a two-step cleavable linker carrying either MMAE or PNU for the desired cytotoxic effect on targeted cells (Fig. 1).

 

Learn more about the GlyCLICK technology for ADC development.

 


 

 

 

GlyCLICK ADC kit MMAE – Site-specific ADC generation with cleavable linker-payloads carrying MMAE.

 

GlyCLICK ADC kit PNU – Site-specific ADC generation with cleavable linker-payloads carrying PNU.