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Showing posts with the label acetylation

MtoZ Biolabs Developed Acetyl-proteomics Analysis Platform

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MtoZ Biolabs , a biotech-company specialized in quantitative proteomics and metabolomics  services, developed a cetyl-proteomics  a nalysis p latform  based on Thermo Fisher's Q ExactiveHF mass spectrometry platform, Orbitrap Fusion mass spectrometry platform, Orbitrap Fusion Lumos mass spectrometry platform and Nano-LC . Acetylation is a highly conserved, reversible protein modification in vivo that plays a n important role in the activation of transcriptional regulators in the nucleus. In addition, a large number of non-histone acetylation modifications are involved in the regulation of metabolic pathways and metabolic enzyme activities. Due to the low content and wide dynamic range of acetylated proteins in biological samples, the acetylated peptides need to be enriched to improve their abundance before mass spectrometry, and then the enriched acetylated groups are obtained by traditional quantitative proteom ics  analysis. The peptide samples are subject...

Part I: Basic Knowledge of Quantitative Analysis of Protein Acetylation Modification

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After the protein is translated in the cell, it is processed through a very important step before being transported to the corresponding organelle and undergoing specific biological effects. The role of protein   post-translational modification   ( PTM ) is primarily to alter the activity, localization or function of the protein. Protein PTM  also further increases the diversity and complexity of cellular pathway mechanisms and life activities. Except for acetylation , c ommon protein PTM  include s   phosphorylation , glycosylation , ubiquitination , and the like. Protein  A cetylation  M odification Protein acetylation modification, as the name suggests, refers to the grafting of acetylated groups on the original basis of the protein. In cells, the acetylation modification reaction is catalyzed by an acetyltransferase, and the acetyl group of acetyl-CoA is transferred and added to the protein lysine residue. In earlier studies, acetylati...