MS Analysis Expert

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 subjected to quantitat

Glycosylation is an important  post-translational modification of p roteins. Glycosylation of proteins can be classified into N-glycosylation and O-glycosylation depending on the manner in which the sugar chain and the peptide chain are linked. N-glycosylation is linked by the N-acetylglucosamine (Glc-NAc) at the reducing end of the sugar chain to the nitrogen atom on the side chain acylamino group of some Asn in the peptide chain. The Asn which can be attached to the sugar chain must be in the motif consisting of the Asn-X-Ser/Thr 3 residue, where X can be any amino acid residue other than Pro. The structure of O-glycosylation is simpler than N-glycosylation, and the sugar chain is generally shorter, but the species is much more numerous than N-glycosylation. The main glycosylation in the peptide chain is Ser and Thr, in addition to tyrosine, hydroxylysine and hydroxyproline, and the linked sites are the hydroxyl oxygen atoms on the side chains of these residues. Based on the h

and drug discovery. The primary structure of the protein molecule itself is the core of its biological function. Therefore, the accurate and rapid analysis of the complete sequence of the protein contributes to the functional study of the unknown protein, and is significant to the development and production of protein drugs including monoclonal antibodies. Traditional protein sequence analysis  technology, whether based on MALDI-TOF mass spectrometer or nanoLC-MS/MS platform, requires the use of a sequence database containing the identified proteins in the protein identification process, and then the molecular weight data measured by mass spectrometry  can be compared to t he molecular weight data obtained after fragmentation of the database theoretical sequence , so as to achieve sequencing and identification of the protein. There are many proteins in the actual protein sequence analysis that are not included in existing databases, such as a new protein that has not been repo