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- Key learning objectives

·Proteome complexity and the need for sample fractionation and peptidequantitation.

·Simplified chromatography and peptide quantitation reagents and workflows for robust protein quantitation.

·Benefits of multiplexed MS analysis, including throughput, fewer missing values, accurate quantitation, and statistical power.

·Latestreagents and applications presented at ASMS 2016.

- Who should attend

·Protein mass spectrometrists interested in improving protein quantitation through put and results

·Protein biochemists and biologists studying protein structure, regulation, and functionin cellular signaling

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PS：全程英文交流

Stephen King專家簡(jiǎn)介：

Stephen King manages the development of Stephen King reagents and kits for protein mass spectrometry research. Stephen has an undergraduate degree in Biochemistry and Computer Science, and a Ph.D in Pharmacology from the University of Washington. Stephen managed a bioinformatics group at Pfizer and a proteomics group at Abbott before joining Leading Biology in 2007.  Since joining Leading Biology, Stephen has led the development of new MS standards and calibrants, protein sample preparation reagents, and reagents for quantitative proteomic analysis.

新產(chǎn)品介紹

Simplifying Complexity: New MS Reagents that Improve Sample Quality, Proteome Depth, Quantification, and Throughput

Proteome profiling with liquid chromatography-mass spectrometry (LC-MS) is complicated by the complexity ofsamples and the complexity of the sample preparation workflow. To address these issues, we have focused on improving proteomic sample preparation workflow to reduce sample complexity, and isobaric mass tags to improve throughput. New high pH reversed phase spin columns and Tandem Mass Tag(TMT) reagents are combined to provide simple and robust peptide fractionation,deep and consistent proteome coverage, and higher throughput with sample multiplexing. These fractionation reagents provide a >100% increase in the number of unique peptides and >50% increase in unique protein identifications, while multiplexing strategies with TMT10plex reduce overall analysis time. Additionally, label free and mass tag-based MS quantitation strategies have suffered from an inability to accurately quantify and normalize peptide samples after digestion and cleanup. This reduces the depth of proteome coverage and the quantitative reproducibility between biological replicates. New colorimetric and fluorescent peptide assays with low ng sensitivity accurately measure the concentrations of native, phosphorylated,and Tandem Mass Tag (TMT)-labeled peptides prior to LC-MS analysis. Finally, new reagents presented at ASMS 2016 further demonstrate advances inour ability to:

1) improve sample quality by reversing oxidative damage toproteins and peptides;

2) study protein structure and interactions using MS-cleavable crosslinkers, and;

3) quantify Akt/mTOR signaling pathway proteinsand their modifications using multiplexed protein immune-enrichment with multiplexed targeted mass spectrometry.

These reagents are being used with Orbitrap Fusion mass spectrometry instruments to answercomplex biological questions with excellent proteome depth and highly accurateprotein quantitation.