Caprion Proteomics is working with Applied Biosystems to accelerate the verification and validation of protein biomarker candidates toward potential use in clinical settings.
Caprion is applying Qtrap technology for the development and deployment of multiple reaction monitoring (MRM) assays to advance the clinical validation of biomarker candidates.
Discovery of a significant number of biomarker candidates in academia and industry has created the need to verify and validate these markers in large-scale projects, to determine the most promising for clinical development.
Caprion specialises in large-scale studies of biomarkers as a service for pharmaceutical and biotechnology companies, as well as for government agencies.
Applied Biosystems provides mass spectrometry technology that complements Caprion's strength in biomarker discovery, to address the need to advance candidates along the biomarker continuum.
Qtrap technology, which was developed by the Applied Biosystems/MDS Analytical Technologies joint venture, enables integrated quantitative and qualitative analysis through the Midas workflow, for fast MRM assay development and accurate quantitative results.
This makes it the technology of choice for Caprion to expand its quantitative capabilities into this rapidly emerging field.
For the many instances, where there are no commercial assays available for a given set of protein biomarker candidates, the MRM technique offers a faster and more cost-effective alternative to established enzyme-linked immunosorbant assay (Elisa) development approaches.
MRM assays can be developed within a matter of weeks, and enable the quantitative parallel tracking of large numbers of biomarker candidates through a multiplex high-throughput format.
This technique has the potential to unlock significant value from the scores of genomics, proteomics and other biomarker candidates that have not yet progressed to the validation stage.
The mass-spectrometry based technique can also prove advantageous in cases where specificity is required, or when specific post-translational modifications or protein isoforms are critical to monitor, but difficult to differentiate by antibody techniques.
