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Tracking protein expression, modifications and interactions with antibody microarrays
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

Tracking protein expression, modifications and interactions with antibody microarrays


6th International Conference & Expo on Proteomics

March 29-31, 2016 Atlanta, USA

Steven Pelech

Kinexus Bioinformatics Corporation, Canada

Scientific Tracks Abstracts: J Proteomics Bioinform

Abstract :

High content antibody microarrays such as the Kinexâ?¢ KAM-900 series chips permit highly sensitive and semi-quantitative analyses of the expressions, post-translational modifications and interactions of proteins with sub-milligram amounts of lysate proteins recovered from cells and tissues. The KAM antibody microarrays utilize at least 878 pan and/or phosphositespecific antibodies for profiling protein kinases, phosphatases and other low abundance cell signalling proteins. Kinexus has developed multiple complementary detection strategies with the KAM chips that enable high depth monitoring of protein levels, phosphorylation and interactions. One method (KAM) involves the capture of in vitro dye-labeled proteins in lysates obtain from cells subjected to diverse treatments. Another method (PAM) involves the detection of general changes in total protein phosphorylation with the pIMAGO stain. A third approach with a dye-labeled reporter antibody in a sandwich antibody microarray format (SAM), for example with our generic phosphotyrosine-specific PYK rabbit polyclonal antibody, allows detection of specific covalent modifications. The SAM method also allows exploration of the interactions of adapter, scaffolding and chaperone proteins with hundreds of potential target signal transduction proteins with dye-labeled reporter antibodies for these highly interactive proteins. Finally, a fourth technique (FAM) utilizes a biotinylated ATP analogue to probe for the accessibility of the ATP binding state in captured protein kinases on KAM chips as a means to determine their possible states of activation. Combining these methods permits a multi-dimension interrogation of the signalling proteomes of cells and tissues and identifies their most dramatic perturbations in response to diverse treatments and pathological conditions.

Biography :

Steven Pelech is the Founder, President and Chief Scientific Officer of Kinexus and previously the Founder and President of Kinetek. His Post-doctoral training was with Sir Philip Cohen at the University of Dundee and Nobel laureate Dr. Edwin Krebs at the University of Washington in Seattle. Since 1988, he has concurrently been on Faculty at the University of British Columbia (UBC) and is a Full Professor in the Division of Neurology. He has received his BSc (1979; Hon.) and PhD (1982) in Biochemistry from UBC. He has authored over 220 scientific peer-reviewed publications about signal transduction. He has served on grant review panels and as a Reviewer for over 30 granting agencies and as an External Reviewer for over 30 scientific journals.

Email: [email protected]

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