BioScale presents data on phospho-protein analysis of MAP kinase pathway activation state at 103rd AACR

BioScale, Inc. a life science company that develops ultrasensitive protein analysis technology, presented findings of recently completed research studies on phospho-protein analysis of the activation state of the MAP kinase pathway at the 103rd Annual Meeting of the American Association for Cancer Research (AACR), held at McCormick Place in Chicago, Illinois, March 31 - April 4, 2012.

“The data we presented at AACR are representative of our commitment to enable advancements in protein research especially in the elucidation of biological pathways so important in cancer research”

"The data we presented at AACR are representative of our commitment to enable advancements in protein research especially in the elucidation of biological pathways so important in cancer research," said Chip Leveille, BioScale's Chief Operating Officer. "Our customers believe that the ability to measure and monitor the activation states and molecular interactions of these pathways are crucial in the understanding and development of anti-cancer pharmaceuticals and therapeutics. Our goal is to provide, through our ViBE workstations and AMMP assay technology, the necessary tools for scientists to identify and ultrasensitively measure the levels of target proteins and biomarkers in complex samples."

The presentation entitled "Snapshot of MAP kinase and related signal transduction pathways from biopsied cells using a novel non-optical assay technology - a proof of concept study" was presented by W. Matthew Dickerson, Ph.D. Senior Assay Development Scientist. The studies reported here utilized non-optical, AMMP (acoustic membrane microparticle) technology to quantitate the activity state of multiple kinases including EGFR, MEK, ERK, AKT, p38 and JNK in their native state and included the detection of the MEK-ERK heterodimer highlighting the ability of the technology to detect weak and transient low affinity interactions. Lysates from multiple unstimulated tumor cell lines were compared with those from the same cell lines specifically stimulated with ligands to several well-known surface receptors for expressed changes in their phosphorylation states. The results indicated that the AMMP assays detect a range of phosphoproteins with improved sensitivity with much simpler workflow. Correlation between protein concentration and cell numbers determined that far fewer than 1000 cells were needed per assessment which is very important when assaying tumor biopsy samples where the cell numbers collected are typically low. And finally, using the AMMP assay, multiple phosphoproteins comprising a portion of the MAPK pathway were measured on a single plate allowing the analysis of groups of analytes at the same time under the same conditions. Monitoring changes in expression of analytes due to stimulation by mitogens or specific agents such as receptor ligands provides significant advantages to drug discovery and development.