Protein Ubiquitination

Ubiquitination, also named as ubiquitylation, is a type of protein post-translational modification by adding ubiquitin to protein sequence. Ubiquitin is a universal regulatory protein that has been found in also all tissues. Ubiquitination modification is divided into two types: monoubiquitination and polyubiquitination, depending the number of ubiquitin molecule linked to proteins. The ubiquitination process contains a multiple enzymatic steps, with sequential action of ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The reaction catalyzed by each enzyme transfers a covalent bond with ubiquitin from one enzyme to the next and finally to a target protein.

Function of ubiquitination:

Ubiquitination has been found to have vital roles in cellular processes including proteasomal degradation, endocytosis, DNA repair, cell cycle regulation, and gene expression. For example, monoubiquitination of cell surface transmembrane receptors target them for endocytosis, and polyubiquitine chains act as scaffolds for ubiquitin-binding proteins, and target them for proteolytic degradation by proteasome. Therefore, when the ubiquitination process is not under proper control, the protein degradation system can be hugely affected, causing protein accumulation and aggregation, which leads to a wide range of human diseases, such as cancer, diabetes, and cardiovascular and neurodegenerative diseases, including Alzheimer’s, Huntington’s and prion diseases.

Workflow of ubiquiitination analysis service:

Ubiquitination Analysis Service

Ubiquiitination analysis service contains:

Creative Proteomics provides a broad range of technologies for ubiquitin research that enable quantification of protein amount and uniquitination modification. You are most welcome to contact us to discuss your project, and we hope we can help to address the challenges in your research.

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Ubiquitination Analysis Service

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