化学
细胞生物学
分子生物学
生物
生物化学
胚胎
作者
Naomi Stolpner,Daniel J. Dickinson
出处
期刊:Methods in molecular biology
日期:2022-01-01
卷期号:: 59-81
标识
DOI:10.1007/978-1-0716-2035-9_4
摘要
Mapping how proteins form complexes and change binding partners is central to understanding cell signaling. Bulk biochemistry can provide a summary of what complexes are present in a cell, but information about the diversity of individual protein complexes is lost. Here, we describe single-cell, single-molecule pull-down (sc-SiMPull), a TIRF microscopy-based coimmunoprecipitation method, to visualize thousands of individual proteins, their binding partners, and protein complex stoichiometry directly from single-cell lysate. By iterating sc-SiMPull over time, temporal dynamics of protein complexes in response to signaling can be constructed.
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