The Consortium for Top Down Proteomics Launches Pilot Project for Characterization of Monoclonal Antibodies

Failed Phd Thesis Twenty-five laboratory study to illustrate the capabilities of top-down mass spectrometry in detailing monoclonal antibody structure and modifications

CAMBRIDGE, MA--(Marketwired - February 28, 2017) - The Consortium for Top Down Proteomics today announced the launch of their inter-laboratory study for characterizing monoclonal antibodies (mAbs) by top-down mass spectrometry techniques. With the continuing growth in the development and adoption of mAbs for a wide range of therapeutic uses, there is increasing demand for higher quality characterization of these complex species.

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Deep and quantitative top-down proteomics in clinical and translational research

Custom University Admission Essay Ohio Summary: It has long been understood that it is proteins, expressed and post-translationally modified, that are the primary regulators of both the fate and the function of cells. The ability to measure differences in the expression of the constellation of unique protein forms (proteoforms) with complete molecular specificity has the potential to sharply improve the return on investment for mass spectrometry-based proteomics in translational research and clinical diagnostics

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A trailblazer in top down proteomics.

A trailblazer in top down proteomics.

Ljiljana Paša-Tolic, better known as Lili, is EMSL's mass spectroscopy capability lead. With a scientific focus in biology, she is particularly interested in the biological applications of mass spectroscopy technology.

Paša-Tolic's primary research area is proteomics – the study of proteins, particularly their structures and functions. Most proteomics research is from bottom up, which means the proteins are broken up and analyzed using liquid chromatography coupled withmass spectroscopy. Bottom up proteomics gives researchers a broad look at the proteins present in the sample, but does not identify the diversity of the protein forms, or proteoforms.

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Top Down Proteomics Consortium meets in Cascais, Portugal

Top Down Proteomics Consortium meets in Cascais, Portugal

Martin Luther King Essays Online The inaugural meeting of the Top Down Proteomics Consortium will be held on March 2-4, 2012 in Cascais, Portugal. David Goodlett (University of Washington, Seattle, WA, USA), Pat Langridge-Smith (University of Edinburgh, Edinburgh, Scotland, UK) and Neil Kelleher (Northwestern University, Evanston, IL, USA) organized a small conference of thought leaders in the field of Top Down Proteomics and representatives of several major instrument vendors to meet and discuss the future of Top Down Proteomics. The overarching goal of this consortium is to construct strong organizational and technical scaffolds that can translate investment in proteomics efficiently into diagnostics and therapeutics to improve human health. The framework we construct together will eventually serve as a vehicle to help deliver on the original promise of the Human Genome Project (1985-2002).

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Kelleher Lab IDs 3,000-Plus Protein Species with New High-Throughput Top-Down Proteomics Platform

Help My Research Paper A team of scientists led by Northwestern University researcher Neil Kelleher has developed a workflow for high-throughput top-down proteomics, using it to identify more than 3,000 protein species in an analysis of HeLa S3 cells.

According to Kelleher, this number of IDs represents a 20-fold increase over any previous top-down experiments in mammalian cells and is one of the first demonstrations of the feasibility of large-scale, discovery-style intact protein work.

New Technique Developed for Top Down Proteomics Quantitation

A "Tandem mass tag protein labeling for top-down identification and quantification." was recently published in Analytical Chemistry. The authors from the Christian-Albrechts-Universität, Kiel, Germany state that "The liberated reporter ions delivered expected ratios over a wide dynamic range independent of the protein charge state. Furthermore, protein sequence tags generated either by low-energy HCD or ETD activation along with the intact protein mass information allow for confident identification of small proteins below 35 kDa."

Top Down ETD Antibody Analysis

Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry.

Source

Biomolecular Mass Spectrometry Laboratory, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland. This email address is being protected from spambots. You need JavaScript enabled to view it.

• Used state of the art ETD-MS/MS instrument (maXis UHR qTOF MS, by Bruker Daltonics)
Characterized two intact recombinant monoclonal antibodies, murine and human IgGs.
The top down ETD data for fragmentation of intact antibodies is superior compared to CID performed on the entire IgG.