Articles by Maria Ekemohn

IgMBRAZOR™ in a Study on Structural Characterization of IgM


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 was observed that digestion of one of the F(ab’)2 subunits occurred more slowly than the other four. It is suggested that interactions of the J-chain within the pentameric IgM structure may influence the accessibility of the IgMBRAZOR enzyme, thus, impacting the digestion kinetics. SEC-CDMS allows the characterization of heterogeneous and large proteins, enabling unique experimental designs such as monitoring of reaction kinetics from physiological buffers.
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Digested Guide to ASMS 2024

May 30, 2024 | Conferences |

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 plan your schedule at ASMS!

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Join our Next GenovisWebinar – Unlock the Power of GlySERIAS™!


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 CQA!

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NEW! We’re Launching TransGLYCIT™ Remodeling Afucosylated Man5!


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 homogenous glycoforms are generated using fast and robust enzymatic workflows.
 
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TransGLYCIT™ in a Study on Antibody Characterization


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.
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Say Hello to IgASAP™ Sub1+2 Lyophilized!

March 25, 2024 | News, Products |

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 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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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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