MS Analysis Expert

No.1 M etabolic L abeling M etabolic labeling strategy is an in vivo labeling method in which cells are "fed" with chemically labeled nutrients that are then incorporated into newly synthesized proteins, nucleic acids or metabolites. We can then collect the cells and isolate these molecules to obtain a global view of the cellular biological processes. Protein  I sotope L abeling Principle: Protein isotope labeling is a classic protein tracing and proteomic quantification technique that replaces the corresponding amino acids in the cell culture medium with essential amino acids labeled with natural isotopes (light) or stable isotopes (heavy), so that newly synthesized proteins can labeling is carried out by incorporation of amino acids containing different isotopes during cell growth. Application example: SILAC ( Stable Isotope Labeling with Amino acids in Cell Culture ) , a stable isotope labeling of amino acids in cell culture is, is a  popular metabolic lab

Although significant advances have been made in genomics, metabolomics, protein and lipid research, glycosylation has not been widely explored at the proteome level. Techniques for analyzing complex glycoproteomes are limited. Glycoproteins differ not only in the number and location of glycosyl groups, but also in the composition and structure of each glycan. Glycoproteomics is one of the most important frontiers in life sciences. In order to overcome the technical limitations in this field, in a new study, Dr. Josef Penninger, director of the Institute of Molecular Biotechnology (IMBA) of the Austrian Academy of Sciences, and his team developed mass spectrometry and algorithms to finally synthesize complex sugar structures and map them to the correct sites for the corresponding glycoprotein. Their newly developed comparative glycoproteomics platform was published online on September 20, 2017 in the journal Nature, entitled Comparative glycoproteomics of stem cells labeled new pla

Based on Thermo Fisher's Q ExactiveHF mass spectrometry platform, Orbitrap Fusion mass spectrometry platform, Orbitrap Fusion Lumos mass spectrometry platform and Nano-LC , MtoZ Biolabs launch ed  protein disulfide bond analysis  solution. Protein identification and structural functional analysis are essential for modern biological research, and mass spectrometry has become a crucial technology for this segment. Many proteins that are localized to the cell surface or secreted extracellularly have disulfide bo nds,  such as antibodies produced by the immune system, various growth factors,   peptide hormones produced by the endocrine system  including, a nd receptors for these growth factors or hormones. Since the correct formation of disulfide bonds is important to the stability and activity of these proteins, and many protein products and target proteins of biopharmaceuticals have these properties, the exact resolution of the disulfide pairing is of great significance to t

With the development of proteomics and biomass spectrometry, large scale quantitative proteomics has become an important aspectof proteomics. Quantitative proteomics  plays important roles in deciphering the biological progress, understanding the development of the disease, and discovering as well as verifying biomarkers for the diagnosis and therapy of diseases. The common quantitative proteomics services are label free and stable isotope labeled quantification , eg. SILAC, iTRAQ. Quantitative p roteomics based on Label Free Label   free  quantification is a method in mass spectrometry that aims to determine the relative amount of proteins in two or more biological samples. Label-free approaches to quantitative proteomics have   gained prominence in recent years since no additional   chemistry or sample preparation steps are required. M ethods :  comparing the ratios of integrated   peak areas/intensities of phosphorylated to nonphosphorylated peptide ions between two sam