Protein Ubiquitination Detection

Ubiquitination is an important post-translational modification of proteins, involved in almost all cellular life activities, making the detection of protein ubiquitination crucial. Biotech company Biotyper provides mass spectrometry-based ubiquitination detection services.Protein Ubiquitination DetectionServices.

Protein Ubiquitination

Protein ubiquitination is a form of post-translational modification of proteins. Ubiquitin is a small (8.6 kDa) regulatory protein found in most tissues of eukaryotic organisms. The process of adding ubiquitin to substrate proteins is termed protein ubiquitination, which involves three main steps: activation, conjugation, and ligation, carried out by ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s) respectively. Protein ubiquitination can be either a single ubiquitin (monoubiquitination) or ubiquitin chains (polyubiquitination). Similar to phosphorylation, ubiquitination is reversible, as ubiquitin can be removed by deubiquitinating enzymes (DUBs). The ubiquitin-proteasome system mediates the degradation of 80%-85% of proteins in eukaryotes. Furthermore, ubiquitination is involved in almost all life activities, including cell cycle regulation, transcriptional regulation, signal transduction, damage repair, and immune response.

Protein Ubiquitination Detection

Protein ubiquitination detection involves determining whether a protein has undergone ubiquitination, identifying the ubiquitination site, and quantifying ubiquitinated proteins. Methods such as western blot, immunoprecipitation, and mass spectrometry can be used to detect protein ubiquitination. Mass spectrometry, by analyzing the mass of enzymatically cleaved peptide fragments, can detect protein ubiquitination, identify the site of ubiquitination via secondary mass spectrometry information, and quantify ubiquitinated proteins through spectral peak intensity.

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Protein Ubiquitination Detection