Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Altered heart rate variability is associated with all-cause mortality in patients with co-morbid insomnia and obstructive sleep apnea.

Sleep·2026

Same author

Mesenchymal stem cells and extracellular vesicles for MAFLD: from biological mechanisms to translational prospects.

Stem cell research & therapy·2026

Same author

Phage enabled precision drug delivery: dual function platforms for therapeutics and genetic cargo transport.

Frontiers in microbiology·2026

Same author

Robotic versus endoscopic breast-conserving surgery: a comparative analysis of clinical outcomes and aesthetic outcomes in breast cancer.

Journal of robotic surgery·2026

Same author

Administration of neuritin as a novel therapeutic strategy for autoimmune and inflammatory diseases.

Molecular therapy : the journal of the American Society of Gene Therapy·2026

Same author

Targeting delayed healing tissues: immune reprogramming of adaptive immune cells by biomaterials.

Regenerative biomaterials·2026

Same journal

Tracking Synthetic Adhesins on Bacterial Surfaces with Immunofluorescence Microscopy.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Post-Selection Methods for Analyzing mRNA Display Selections and Optimization of Hits.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

High-Performance Computing in Tandem Mass Spectrometry (MS/MS) Peptide Identification.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Engineering and Adapting Disulfide-Containing Proteins to Enable Intracellular Functionality.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

AI-Driven Protein Research: From Prediction to Design.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Methods for the In Vitro Selection of Protein and Peptide Libraries Using mRNA Display.

Methods in molecular biology (Clifton, N.J.)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Aug 27, 2025

Detection of Protein Ubiquitination

Detection of Protein Ubiquitination

Published on: August 19, 2009

Protein Ubiquitination Assay.

Ping Wei^1,2, Rui Liang¹, Fan Pan³

¹Shenzhen Institute of Advanced Technology (SIAT), Chinese Academy of Sciences (CAS), Shenzhen, People's Republic of China.

Methods in Molecular Biology (Clifton, N.J.)

|September 30, 2022

Summary

This summary is machine-generated.

Ubiquitin modification of FOXP3, a key immune regulator, is investigated. This posttranslational modification, detected via His pull-down and immunoprecipitation, impacts immune signaling and protein stability.

Keywords:

Covalent bond Pull-down assay Ubiquitination

More Related Videos

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Related Experiment Videos

Last Updated: Aug 27, 2025

Detection of Protein Ubiquitination

Detection of Protein Ubiquitination

Published on: August 19, 2009

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Area of Science:

Molecular Biology
Immunology
Biochemistry

Background:

Ubiquitin is a 76-amino acid protein crucial for protein regulation.
Ubiquitination is an enzymatic cascade involving E1, E2, and E3 enzymes.
FOXP3 is a critical transcription factor in immune regulation.

Purpose of the Study:

To investigate the ubiquitination of FOXP3.
To understand the role of FOXP3 ubiquitination in immune responses.

Main Methods:

Histidine (His) pull-down assays.
Immunoprecipitation (IP) assays.

Main Results:

FOXP3 ubiquitination was successfully detected using His pull-down and IP assays.
Ubiquitination represents a significant posttranslational modification of FOXP3.

Conclusions:

FOXP3 ubiquitination is a key regulatory mechanism in immune cells.
This modification may influence signal transduction pathways.
FOXP3 ubiquitination could lead to 26S proteasome-dependent degradation.