Articles in the Category ”Products”

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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GlycINATOR® in Peptide Mapping of Fc Domain-Drug Conjugates


The field of antibody-drug conjugates (ADCs) is rapidly emerging as a new, important class of cancer therapeutics. ADCs consist of monoclonal antibodies (mAbs) covalently linked to cytotoxic drugs, and after selective surface receptor binding on cancer cells, the drug is delivered into the intracellular compartment and can exert its cytotoxic effect.
 
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GingisREX® in a Bottom-Up Analysis of Histones


Bottom-up mass spectrometry where the intact protein is digested into smaller peptides is an indispensable tool for proteomics and the studying of histone codes. Since histones are enriched with the basic amino acids arginine and lysine, enzymatic digestion is often challenging as peptides too short for LC retention and PTM localization are generated. In addition, the complex workflow entails that the combination of samples preparation, data acquisition and analysis provides a different image of the histone code.

 

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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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Purification of Antibody Fragments via Hydrophobic Interactions


The importance of monoclonal antibodies (mAbs) as therapeutic agents is steadily increasing, and each year nearly 300 novel mAbs are being evaluated for their therapeutic effectivity. Interest has also been expressed in the use of antibody fragments as therapeutic agents. The physiochemical properties of the fragments differ significantly from that of intact antibodies, and the fragments can more easily be coupled to dyes, toxins and vesicles for diagnostic purposes, cancer therapy and improved drug delivery, respectively.
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Analytical Methods to Monitor Site-Specific ADC Generation with GlyCLICK®


Scientists at the University of Strasbourg and University of Geneva use innovative native MS and IM methodologies for analytical characterization of a site-specific ADC generated with the GlyCLICK technology.

 

Antibody-drug conjugates (ADCs) combine the benefits of tumor-targeting monoclonal antibodies with the cytotoxic effect of drug payloads covalently linked to the antibody. The ADC generation process has evolved from non-selective and uncontrolled conjugation in early generation products, to site-specific conjugation resulting in homogenous and well-defined ADCs. Conjugation at the antibody Fc glycan sites using the GlyCLICK technology has proven to be an attractive option for the generation of site-specific ADCs.
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FabALACTICA Facilitates the Structural Insight into SARS-CoV-2 Neutralizing Antibodies


The first steps of infection with SARS-CoV-2 is binding of a viral Spike protein to a host receptor angiotensin-converting enzyme 2 (ACE2), followed by fusion of viral and host membranes. Antibodies that block this interaction are emerging as early COVID-19 therapies, however, the neutralization potencies of the antibodies are less studied.
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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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Automated Biotransformation Analysis of ADCs using FabRICATOR

The development of antibody-drug conjugates (ADCs) has evolved from first generation formats prepared by random conjugation technologies to next generation ADCs generated by site-specific conjugation. While significant improvements in overall efficacy and safety is displayed by site-specific formats, bioanalysis remains challenging due to complex in vivo biotransformation events including deconjugation, linker-payload cleavage and payload metabolism.

 

In this work, scientists at Bristol-Myers Squibb describe the development of an automated and fast affinity capture method using a cartridge-based platform combined with LC-HRMS analysis for biotransformation assessment of site-specific ADCs.

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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.