J. Vallaghé1, D. Monchiet1, N. Costy1, T. Chardès2, C. Larbouret2, E. Trinquet1, F. Charrier-Savournin1
1 Cisbio Bioassays, Codolet, France | 2 Institut de Recherche en Cancérologie de Montpellier, INSERM U896, Université Montpellier 1, Institut régional du Cancer Montpellier / Val d’Aurelle, France
Cell signaling pathways involving phospho-proteins are often over-activated in cancers, leading to aberrant cell proliferation and survival. Therefore, protein phosphorylation is frequently assessed while developing novel anti-tumor therapeutics, such as tyrosine kinase inhibitors (TKI) or monoclonal antibodies. In preclinical cancer studies, human tumor xenograft-bearing mice are routinely used as predictive models to evaluate the in vivo efficacy of such anticancer drugs. Western blot is the standard technique for analyzing proteins in tumor lysates, but it is time- and labor-intensive.
This poster compares the use of HTRF phospho-assays with traditional Western blot for the analysis of AKT and ERK1/2 in human pancreatic tumor xenografts, after mouse treatment with the anti-EGFR TKI erlotinib. The data demonstrates that HTRF is a more convenient, accurate and sample-saving method than Western blot for assessing protein phosphorylation in tumor xenografts.