Protypia offers analytical solutions for drug safety and therapeutic development.
Daniel C. Liebler is President and Founder of Protypia, LLC and Adjunct Professor of Biochemistry at the Vanderbilt University School of Medicine. Dr. Liebler’s research program has focused for 30 years on the application of analytical technology, particularly mass spectrometry, to study the interactions of chemicals with biological systems. His group has made important contributions to the fields of antioxidant chemistry, toxicology mechanisms, proteomics, chemical biology and cancer proteogenomics. Dr. Liebler has authored 295 peer reviewed publications.
Quantitative analysis of proteins by mass spectrometry provides precision, accuracy and dynamic range unavailable with immunoassay platforms and also enables simultaneous measurement of multiple proteins in a sample. Samples include frozen and FFPE tissues or cells and typically require approximately 100 micrograms of protein (1-2 mg wet weight for fresh./frozen; 1 e6 cells; or 1 cm diameter, 5 micron thickness FFPE section). A principal focus of Protypia is analysis of proteins that control the tumor-immune interface and are immune-oncology (IO) drug targets or critical co-regulators immunotherapeutics. The Protypia platform can simultaneously measure immune checkpoints, co-regulators and immune cell markers, as well as tumor and stromal markers. IO assay menu of over 25 proteins includes PD-L1, PD-L2, LAG3, IDO1, TIM3, VISTA. Incorporation of additional targets upon request. In addition to IO protein panels, multiplexed protein analysis panels focused on other pathways are available.
Quantitative shotgun proteomic analysis provides unbiased survey of protein abundance difference between cell and tissue samples representing distinct phenotypes, disease states, responses to drugs and drug and chemical toxicity. Analysis of 100 micrograms of protein (1 e6 cells; 1-2 mg wet weight frozen tissue; 1-2 FFPE unstained sections of 1cm diameter and 5 micron thickness) typically yields 6,000+ protein identifications. Quantitative estimates of abundance differences of > 2-fold are typically achieved. Shotgun proteomics identifies candidate biomarkers, pathway alterations and changes in gene expression, including unanticipated alterations not manifested at the transcriptome level. Integrative analysis of shotgun proteomics data with genomic, transcriptomic, copy number or other data types enables assessment of multi-level gene regulation.
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