Friday, April 18, 2014


Research in the Ong Lab for Quantitative Biology

Mass spectrometry (MS)-based proteomics is a uniquely powerful and versatile tool in biology as it allows unbiased, comprehensive and sensitive detection of proteins in complex mixtures. With the ability to identify thousands of proteins in a single experiment, MS-based proteomics makes it easy to generate lengthy protein catalogs, but qualitative comparisons of lists of proteins is less informative. Instead, the ability to measure abundances of specific proteins and observe these changing over time in response to a defined perturbation is extremely powerful. Such information can be obtained with quantitative proteomics, which greatly enhances the power and utility of MS-based methods.

We use chemical labeling methods, like iTRAQ or metabolic labeling with SILAC, to quantify changes in protein abundance, enabling functional assays to compare protein expression levels in perturbed and control cell states. In SILAC, proteins from two cell populations labeled with normal isotope abundance or stable isotope labeled amino acids are observable in the same mass spectrum and distinguishable by their respective "light" and "heavy" peptide signals. This transforms the proteomic experiment into a format akin to a microarray experiment: when samples are mixed in equal proportions, signals from both populations are detectable unless the absence of either the light or heavy member is a direct result of the experimental perturbation. With this method, protein expression changes can be modeled and significant changes called with high confidence. Issues related to stochastic sampling of control-experiment pairs that plague classical proteomic approaches are avoided altogether. Along with dramatic improvements in the speed and sensitivity of MS instruments over the last decade, these quantitative methods have enabled impressive proteomics studies like the comprehensive identification of proteins in sub-cellular organelles like mitochondria and nucleoli, and quantification of subtle changes in whole proteomes induced by microRNA overexpression.

Our laboratory focuses on the development of novel approaches to study functional roles of protein complexes; particularly the dynamics of their formation and recruitment, abundances and post-translational modifications in cellular signaling, growth and proliferation.


Welcome Sabrina!

Sabrina Kamran joins the Ong lab for a rotation in Spring 2014. Welcome Sabrina!

Current recruitment drive!

Are you our new Post-doc?

The Ong Lab is looking for creative and talented post-doctoral fellows to join the lab!

Our research group is looking for a postdoctoral fellow to join our team. We use mass spectrometry-based quantitative proteomics to study protein complexes in signaling and gene regulation. Our research is at the interface of proteomics, chemical biology, and genomics and seeks to understand biological processes at a systems level through the development and application of new proteomics methods.

POSITIONS AVAILABLE:  We have open positions for post-doctoral and pre-doctoral level scientists. Position requirement: Outstanding analytical or computational skills, expertise in biochemistry or molecular biology. A background in developmental biology, chemistry, cell biology, genetics or epigenetics would be preferable.

Email a cover letter and your CV to Shao-En.

A streamlined workflow to profile kinase inhibitor targets

Our new paper describing a rapid and streamlined workflow to characterize targets of protein kinase inhibitors is now out in the March 2014 issue of Med Chem Communications. The protocol allows a single operator to characterize a small panel of six small molecule probes in a week! Here's the link to the paper in MedChemComm.

Welcome Emily!

Emily Myers, Class of 2013 UW Pharmacology, will rotate in the Ong lab over Winter quarter 2013.

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