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Rapid Generation of Accurate Information on Proteoform Distribution and Relative Abundance by UHR-QTOF MS

Rapid Generation of Accurate Information on Proteoform Distribution and Relative Abundance by UHR-QTOF MS

24 Dec 2015

Over their life cycle, proteins undergo various transformations that can alter their functions while keeping a good part of their primary sequence intact. This multiplication of Post Translational Modifications (PTM) patterns, alternative splice forms or products of proteolytic processing cannot be easily resolved with a bottom-up approach, as very few peptides are specific from a given proteoform. However, the information relative to the distribution of different proteoforms can be seen in their intact mass profile. This application note explores the potential of the latest generation UHR-QTOF to quickly map the distribution and relative abundances of proteoforms in complex protein extracts.

Impact II

Bruker Daltonics

 Robustness to sample variation, low picogram sensitivity, and simplicity in delivering highly precise and reproducible MS and MS/MS data without the need for tuning or optimization.

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Mass SpectrometryMass spectrometry (MS) is a powerful analytical technique used to identify and quantify molecules based on the mass-to-charge ratio of gas-phase ions. It provides detailed information about the structure, composition, and properties of compounds and is widely used across fields such as environmental monitoring, materials science, drug discovery and development, food and beverage testing, and wider chemical research. Key MS techniques include tandem mass spectrometry (MS/MS), liquid chromatography–mass spectrometry (LS-MS) and inductively coupled plasma (ICP-MS). Choosing from these wide range of techniques and technologies can be a daunting task, so keep up to date with scientific applications, performance expectations, and customer reviews here all in one place. Visit our product directory to receive quotes direct from the manufacturer. Protein PurificationProtein purification is a vital step in drug discovery, therapeutics, biotech and life science research. The purification process typically involves subcellular or membrane protein extraction with cell lysis kits, separation of proteins from cell debris by filtration or spin columns, and the isolation of proteins of interest from other proteins and impurities with affinity purification (including fusion protein tags and antibody binding proteins A, G and L), immunoprecipitation or chromatographic methods, such as ion exchange, size exclusion and immobilized metal affinity chromatography. All purification methods come in multiple formats for your laboratory needs, including agarose or magnetic beads, resins, columns and filter plates. Find the best protein purification equipment in our peer-reviewed product directory: compare products, check customer reviews and receive pricing direct from manufacturers.ProteomicsProteomics is the systemic bioinformatics study of proteins and amino acids, including their structure, size, function and identification. Tools used in proteomics include chromatography, blotting and gels, protein arrays, mass spectrometry and ELISA and associated analysis software. Analyzers and proteomic systems should be sensitive, high resolution, fast and may be automated for high-throughput.Protein InteractionsProtein interactions are essential for understanding cellular processes, as proteins work together to carry out biological functions. Studying protein interactions can provide insights into disease mechanisms, drug development, and cell signaling pathways. Explore the best tools for protein interaction research in our peer-reviewed product directory; compare products, check reviews, and get pricing directly from manufacturers.Peptide MappingPost-Translational ModificationsProtein Quantification
Rapid Generation of Accurate Information on Proteoform Distribution and Relative Abundance by UHR-QTOF MS