演題概要

ポスター発表

第3日 5月16日(金)  会場(月光)

定量リン酸化プロテオミクスによる標的パスウェイのリン酸化動態解析

(京大院薬)
o矢崎達也高木俊輔若林真樹杉山直幸石濱泰

Phosphorylation is an essential regulatory mechanism to control various cellular functions. Quantitative phosphoproteomics is a powerful tool to monitor the entire map of cellular phosphorylation of proteins, in order to understand the comprehensive biological functions. However, even after phosphopeptide enrichment, we found that the complexity of phosphoproteome samples is high enough to cause the ionization suppression, the reduction of peak purify and the inaccurate quantitaion. In this study, we focused on Her2 and its downstream molecules, and evaluate the influences of high resolution/accuracy in LC, MS and MS/MS on accuracy and sensitivity in targeted quantitative phosphoproteomics.