PerkinElmer launches powerful trio of proteomic research technologies at 2006 HUPO World Congress

2 Nov 2006
Kerry Parker
CEO

PerkinElmer, Inc., a global leader in Health Science and Photonics, today announced it is significantly enhancing its portfolio of proteomic research tools with the launch of three powerful new technologies: ExacTag™ mass tags, Phos-tools™ and Affinity-tools™. PerkinElmer will launch and display these new research technologies during the Human Proteome Organization’s (HUPO) Fifth Annual World Congress, October 28 through November 1, 2006, Booth #236, Long Beach, CA.

ExacTag™ mass tags are a family of thiol and amine reactive isobaric mass tags that offer flexibility for the quantification of protein expression of up to 10 samples simultaneously, significantly improving productivity and enabling analysis of protein expression pharmacodynamics. Phos-tools, consisting of the Phos-trap™ and Phos-tag™ products, provide a high selectivity for the enrichment and detection of protein phosphorylation. Affinity-tools allow for the selective isolation of proteins of interest and sensitive detection by gel resolution or by mass spectrometry. All products are compatible with common mass spectrometry (MS) work flows.

ExacTag™ provides a superior approach over current technologies for determining the relative expression levels of individual proteins. “These current technologies mostly rely on the differential display of protein expression,” noted Richard Eglen, vice president and general manager of the Discovery and Research Reagents business unit of PerkinElmer Life and Analytical Sciences. “ExacTag mass tags allow more samples to be processed simultaneously, enhancing productivity and enable drug discovery laboratories to perform pharmacological analysis of cellular protein expression.

PerkinElmer Phos-tools™ utilize unique chemistries to provide a high binding selectivity for phosphorylated tyrosine, serine and threonine residues. “Most functional cellular activities are wired through phosphorylation cascades that are triggered by kinases and phosphatases,” stated Eglen. Kinases are some of the most exciting drug targets in today’s pharmaceutical research and this suite of tools allows scientists to isolate and detect phosphorylation events with significantly enhanced sensitivity and selectivity over current IMAC technology. “Identifying phosphoproteins and their sites of phosphorylation provides a wealth of information necessary for designing the next generation of drugs suitable for the personalization of medicine,” added Eglen.

PerkinElmer’s Affinity-tools™ offer a selection of protein enrichment and detection kits based upon conventional immuno- and biotin-binding protein capture strategies. The tools have been specifically designed with elution buffers that are compatible with all mass spectrometry ionization sources. “One application we are particularly excited about,” noted Eglen, “involves the rapid enrichment of plasma membrane proteins for both gel and MS detection. This should prove extremely useful for target discovery and validation studies of these most pharmaceutically treatable therapeutic targets.”

More information about these innovative new platforms for proteomics research is available at the article webpage.

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