LC-MS/MS Peptide Mass Spectrometry Analysis of Ubiquitination Sites
Ubiquitination is a prevalent post-translational modification instrumental in regulating numerous cellular processes, including protein degradation, signal transduction, and protein subcellular localization. Consequently, precise identification and localization of ubiquitination sites are of great biological significance. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) is a pivotal analytical technique used in the identification of ubiquitination sites. This technique integrates liquid chromatography (LC) with tandem mass spectrometry (MS/MS) to separate sample components via LC before conducting mass spectrometric analysis in the MS/MS analyzer. By analyzing the resultant mass spectra, distinct components can be accurately identified.
The Application of LC-MS/MS in Ubiquitination Site Identification Involves the Following Steps
1. Protein Digestion
Ubiquitinated proteins are initially digested into peptides using enzymes such as trypsin.
2. Peptide Separation
The resultant peptides are separated through LC.
3. Mass Spectrometry Analysis
Subsequently, these peptides undergo MS/MS analysis, whereby the amino acid sequences and modification sites are determined from the mass spectra obtained.
This methodology enables the precise identification of ubiquitination sites, thereby enhancing our comprehension of the role ubiquitination plays in biological processes.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
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