2. Academic Validation
  3. Protein Ubiquitination Assay

Protein Ubiquitination Assay

  • Methods Mol Biol. 2023:2559:137-149. doi: 10.1007/978-1-0716-2647-4_10.
Ping Wei 1 2,  Rui Liang 1,  Fan Pan 3
Affiliations

Affiliations

  • 1 Shenzhen Institute of Advanced Technology (SIAT), Chinese Academy of Sciences (CAS), Shenzhen, People's Republic of China.
  • 2 Department of Otolaryngology, Ministry of Education Key Laboratory of Child Development and Disorders, National Clinical Research Center for Child Health and Disorders (Chongqing), China International Science and Technology Cooperation Base of Child Development and Critical Disorders, Children's Hospital of Chongqing Medical University, Chongqing, China.
  • 3 Shenzhen Institute of Advanced Technology (SIAT), Chinese Academy of Sciences (CAS), Shenzhen, People's Republic of China. fan.pan@siat.ac.cn.
PMID: 36180631 DOI: 10.1007/978-1-0716-2647-4_10
Abstract

Ubiquitin, a 76-amino acid protein which could covalently bind to a target protein, is catalyzed by an enzymatic cascade comprising of ATP-dependent ubiquitin-activating Enzyme E1, ubiquitin-conjugating Enzyme E2, and ubiquitin-protein Ligase E3. Histidine (His) pull-down and immunoprecipitation (IP) assays are frequently adopted to detect FOXP3 ubiquitination, which is one of the most important posttranslational modifications and may induce signal transduction or 26S proteasome-dependent degradation of FOXP3 in various immune milieus.

Keywords

Covalent bond; Pull-down assay; Ubiquitination.

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