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To understand what makes a cell function normally and what may go awry in disease, we need better tools and resources, such as renewable protein capture reagents and probes, to study how proteins work in isolation and how they interact with other proteins, carbohydrates, or DNA regions within a cell. Ideally, we would have a library of protein capture reagents that would allow us to identify and isolate all proteins within cells – the so called “proteome” – to ensure broad application in research and clinical studies aimed at understanding, preventing, detecting and treating disease. Existing renewable protein capture reagents, such as monoclonal antibodies, have been developed for a number of protein targets, although these represent only a subset of all proteins comprising the human proteome. In addition, many monoclonal antibodies lack the desired level of specificity because they do not reliably target only the protein of interest. This is particularly problematic given the multiple forms assumed by any one protein and the broad range of protein types in the body.

A renewable resource of protein capture reagents – specifically designed to meet research and clinical demands ranging from protein isolation and high-throughput assays to diagnostics and biomarker development – is needed to advance the field of proteomics and fuel biomedical research. To have the maximum benefit, such reagents would need to be high quality, affordable, reliable monoclonal antibodies and other reagents that can collectively target the range of possible proteins within cells and tissues. But what do these reagents look like and how can they be developed, optimized and scaled for use in large-scale proteomics research and clinical applications? The Common Fund Protein Capture Reagents program seeks to address these questions and establish a “protein capture” resource of reagents for the biomedical community. See: Program Highlights for more information and ProteinCapture.org Exit Disclaimer for the reagents that are currently available.

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