通过免疫共沉淀技术鉴定病毒 E3 连接酶识别的泛素化衔接蛋白。
Identifying a Ubiquitinated Adaptor Protein by a Viral E3 Ligase Through Co-immunoprecipitation.
机构信息
State Key Laboratory of Antiviral Drugs, Pingyuan Laboratory, NMPA Key Laboratory for Research and Evaluation of Innovative Drug, School of Chemistry and Chemical Engineering, Henan Normal University, Xinxiang, Henan, China.
Department of Nephrology and Rheumatology, The Second Affiliated Hospital of Zhengzhou University, Zhengzhou, Henan, China.
出版信息
Methods Mol Biol. 2025;2854:35-40. doi: 10.1007/978-1-0716-4108-8_5.
Co-immunoprecipitation is a technique widely utilized to isolate protein complexes and study protein-protein interactions. Ubiquitinated proteins could be identified by combining co-immunoprecipitation with SDS-PAGE followed by immunoblotting. In this chapter, we use Herpes Simplex Virus 1 immediate-early protein ICP0-mediated polyubiquitination of p50 as an example to describe the method to identify a ubiquitinated adaptor protein by a viral E3 ligase by co-immunoprecipitation.
免疫共沉淀是一种广泛用于分离蛋白质复合物和研究蛋白质-蛋白质相互作用的技术。通过将免疫共沉淀与 SDS-PAGE 结合，再进行免疫印迹，可以鉴定泛素化蛋白。在本章中，我们以单纯疱疹病毒 1 早期蛋白 ICP0 介导的 p50 多泛素化为实例，描述了利用病毒 E3 连接酶通过免疫共沉淀鉴定泛素化衔接蛋白的方法。
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