Genovis Certified to ISO 9001:2015
We are proud to annouce that we are certified to ISO 9001:2015!

Welcome to our blog! This is where we share a bit more – insights, updates, and thoughts from Genovis. Take a look around and see what you find.

Search post
Category
We are proud to annouce that we are certified to ISO 9001:2015!

In a recent article by Srzentic et al. (2018) the authors present a multiplexed middle-down MS workflow with improved performance for targeted protein structure analysis. Using GingisKHAN for antibody digestion, the authors analysed the F(ab) subunits of a therapeutic mAb. By implementing spectral and transient averaging of mass spectra across several LC-MS experiments,…

In an article by Luca Fornelli & Kristina Srzentic et al. recently published in Analytical Chemistry the authors present a workflow for antibody sequence determination by combining top-down and middle-down LC/MS. The authors analyzed the therapeutic antibody rituximab in its intact and fragmented form, using FabRICATOR and GingisKHAN to generate antibody subunits. By combining the…

In an article by Stroll et al. (2018), the authors demonstrate a striking in-depth characterization of three therapeutic mAbs, achieved by combining FabRICATOR® (IdeS) digestion with an online two-dimensional LC-MS approach. The authors generate a highly resolved separation and detection of FabRICATOR-digested N-glycosylated mAb subunits by implementing Active Solvent Modulation (ASM), a method for valve-based…

Genovis is expanding its sales and marketing organization at its Lund headquarters and has hired Rob Horsefield as Sales & Business Development Manager. Rob has multiple years of experience in the industry from sales in analytical chemistry, pharmaceutical development and protein chemistry. We are happy and proud to have you on board, Rob. Welcome to…
Scientist at the Center for Biologics Evaluation and Research, Food and Drug Administration, have, in collaboration with Genovis, developed a method for analyzing O-glycosylated proteins based on a solid phase chemical modification and followed by OpeRATOR digestion. Using this method, up to 8-fold more O-glycosites were discovered as compared to previously reported data. …
Several researchers have submitted abstracts for ASMS 2018 in San Diego, in which Genovis' SmartEnzymes have been used. Below is a selection of these abstracts. To read the poster abstracts, visit the Online Planner for ASMS, and paste the abstract titel in the search field. Monday June 4 10:30AM-2:30PM: Poster Session MP 045 - GlyCLICK Development…

Unique enzymatic digestions in study of antibody disulphides Valegh Faid and colleagues at LFB Biotechnologies in France have developed and published an assay to study antibody disulphide bonds using middle-up LC-MS (Faid et al., 2017). The combination of FabRICATOR® for digestion below the hinge and FabALACTICA™ for digestion above the hinge, generated three…
We are happy and proud to have you on board, Kevin. Welcome to Genovis! Tell us a bit about yourself. Even though a Focused Generalist does not make perfect sense, I think it fits since I have a broad life sciences discovery background with a specificity towards LC-MS and orthogonal technology. If…

In a study by Wohlschlager et al. (2018), FragIT™ kit was used to digest the Fc-fusion protein etanercept, and the resulting fragments were analyzed using high-resolution native mass spectrometry (MS). Native MS offers a higher spatial resolution at a lower charge state, enabling studies of glycan heterogeneity, and FragIT digestion reduces sample complexity, enabling a…

Please welcome GlycOCATCH™ to the Genovis SmartEnzymes™ family! GlycOCATCH is an enrichment resin for affinity purification of O-glycosylated proteins and peptides. The resin is designed to bind proteins and peptides carrying O-glycans with high affinity, and it is provided in convenient spin columns to allow easy-to-use O-glycoprotein enrichment. The applications of GlycOCATCH involve…

Hydrophobic interaction chromatography (HIC) is often used in characterization of therapeutic antibody products due to its ability to separate direct or indirect structural changes in the studied protein. Scientists at Alexion have published a study where FabRICATOR (IdeS) was used to generate Fc and F(ab’)2 fragments of an antibody to study conformational changes of a monoclonal…