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    Acetylation Modified Proteome

      Protein acetylation is the process by which an acetyl group is covalently attached to lysine residues by enzymatic or non-enzymatic means with acetyl group donors (such as acetyl coenzyme A), which is a very important post-translational modification of proteins. Protein acetylation plays a crucial regulatory role in protein-related processes such as apoptosis, subcellular localization of proteins, protein-DNA interactions, DNA replication and repair, and DNA transcriptional activity, and has become one of the hot spots in the study of modified proteomics in recent years.

       

      The study of proteomics not only provides a material basis for the analysis of life activity rules, but also provides theoretical basis and solutions for elucidating and conquering many diseases. The study of acetylated modified proteins from the perspective of proteomics mainly focuses on the large-scale qualitative and quantitative identification of acetylation modification and modification sites. The general process is to use acetylation antibodies to enrich acetylated peptides in mixed samples, then identify them through mass spectrometry, and then judge whether lysine residues or N-termini of proteins are acetylated by comparing the mass difference of +42Da in experimental and theoretical peptide mass spectra. At the same time, further analysis of b or y ions from the N- and C-termini of individual peptides can determine the amino acid site of acetylation. Finally, bioinformatics analysis is used to find acetylated proteins, screen proteins with biological significance, and study protein biological functions. The study of the acetylated modified proteome not only reveals a new dimension of protein function for us, but also provides a powerful tool for us to deeply understand cell biology processes and disease development. With the continuous development of technology and deepening research, the acetylated modified proteome will play an increasingly important role in the field of biomedicine.

       

      MtoZ Biolabs uses Thermo Fisher's Q ExactiveHF mass spectrometer platform, Orbitrap Fusion mass spectrometer platform, Orbitrap Fusion Lumos mass spectrometer platform combined with Nano-LC, and launches an analysis service package for acetylated modified proteome. You just need to tell us your experimental objectives and send your samples to us, and we will be responsible for all subsequent matters of the project, including protein extraction, protein enzyme cutting, enrichment of acetylated peptides, peptide separation, mass spectrometry analysis, analysis of mass spectrometry raw data, and bioinformatics analysis. Feel free to consult for free.

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