Articles in the Category ”News”
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!
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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NEW! We’re Launching PNGase F Automation!
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!
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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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
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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NEW! We’re Launching GlySERIAS Immobilized
GlySERIAS is a unique enzyme that digests flexible glycine-rich fusion protein linkers such as Gly4Ser and GlyxSery (GS), and polyglycine (G) linkers. Today, we’re happy and proud to be launching this unique SmartEnzyme in a new format – GlySERIAS Immobilized – for digestion of flexible linkers in easy-to-use spin columns!
The enzyme enables separation of the individual domains of multi-functional fusion proteins to facilitate characterization and increase the understanding of these molecules. Middle-level analysis of fusion proteins serves to both reduce the overall sample complexity and allow for domain-specific identification and monitoring of post-translational modifications.
For improved linker removal, we recommend GlySERIAS Immobilized.
For linker characterization, we recommend GlySERIAS Lyophilized.
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It’s Time for a Change!
As part of our overall strategy to become even more sustainable and caring for the environment, we are updating our product boxes (see below). When updating the boxes, we also want to make it easier for you to know what you get when you buy or search for a product from us. We are therefore creating a clearer structure regarding our product naming!
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