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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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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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.
Dissertation Themes 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.
Once published, you will have a stable "Uniform Resource Identifier" to include with your journal publication and we will link to it from the Consortium's Datasets Page, http://topdownproteomics.org/data. An example of a published dataset can be found here: http://topdownproteomics.org/data/item/ultraviolet-photodissociation-for-characterization-of-whole-proteins-on-a-chromatographic-time-scale.