Agilent Technologies Introduces New Complex Proteomics Standard at HUPO 8th Annual World Congress
TORONTO, HUPO 8th Annual World Congress.-Agilent Technologies Inc. (NYSE: A) today announced the new Agilent Complex Proteomics Standard, created to help researchers with protein biomarker discovery by validating mass-spectrometry-based workflows for protein identification. It is the most advanced standard for MS-based proteomic workflow qualification testing.
The Agilent Complex Proteomics Standard was developed in collaboration with thought leaders Dr. Ruedi Aebersold, of ETH Zurich, and Dr. John Yates III, of the Scripps Research Institute. Currently, this is the only proteomics standard able to mimic the complexity and diversity of a typical proteomic sample - useful for benchmarking different proteomic workflows and for workflow validation over time, across multiple instruments and across laboratories.
“This technology represents the first truly complex proteomics standard, which will provide proteomics researchers a control to assess, compare and quality-control their experimental methodologies,” said Dr. Yates.
The Agilent Complex Proteomics Standard is applicable to a wide range of LC/MS-based applications and can be used with the Agilent 1200 series LC and 6000 series MS systems as well as MS instruments from other suppliers.
“In contrast to existing standards, the Agilent Complex Proteomics Standard can represent the complexity and diversity of real proteomic samples, such as protein mixtures derived from serum, CSF, urine or tissue,” said Bill Molnar, general manager of Agilent’s genomics division. “The high number of proteins from a single organism with a fully sequenced genome allows researchers to extensively qualify LC/MS workflows with regard to all aspects of sample preparation, data acquisition and analysis, including database search.”
The Agilent Complex Proteomics Standard contains more than 1,500 proteins covering a wide range of protein sizes/molecular weight, pI and hydrophobicity. Genetic distance between Pyrococcus furiosus and human (or other organisms typically subjected to proteomic studies) helps avoid erroneous protein identification.
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