MS Analysis Expert

Mass spectrometry is sensitivity and accura te , and can accurately identify proteins. At present, mass spectrometry mainly identifies the primary structure of egg, including molecular weight, amino acid sequence of peptide chain and number and position of polypeptide or disulfide bond, which plays an important role in the study of protein structure analysis. Mass spectrometry consists of injector, ion source, mass analyzer, ion detector, control computer, and data analysis system. Traditional mass spectrometry is only used for the analysis of small molecule volatiles, but with the emergence of new ionization techniques such as matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and electrospray ionization mass spectrometry (ESI-MS) , e tc . Th e emergence of various mass spectrometry techniques provides a new and accurate way for protein analysis . Now,  the combined application of enzymatic hydrolysis, liquid chromatography separation,...

The rapid development of metabolomics, especially the advances in analytical techniques, increased sample size, diversification of sample types, and the combined use of multiple detection platforms have dramatically increased the number and complexity of metabolome data. The development of metabolomics databases has important implications for summarizing these big data, increasing data usage, conducting deep   analysis, and revealing the biological mechanisms behind big data. Currently, the databases involved in metabolomics  research can be roughly divided into two levels , the original database that stores the raw test data and the metabolite library that stores information about metabolites and metabolic pathways. The earliest and relatively mature is the metabolite library. The early metabolite librar ies are primarily basic information for storing various metabolites, including profiles of metabolites, chemical formulas, molecular weights , chemical classifications, ...

Protein Q uantum D ot L abeling Principles: Quantum Dots is an inorganic nanocrystal that emits fluorescence at a specific wavelength according to its size. It has a very high extinction coefficient and its extinction coefficient is 10 to 100 higher than that of small molecule fluorophores and fluorescent proteins. The quantum yield of quantum dots is also good. Typical quantum dots contain a cadmium selenide (CdSe) or cadmium telluride (CdTe) core surrounded by a zinc sulfide (ZnS) shell. Quantum dots absorb a wide range of wavelengths from very short wavelengths to slightly below their emission wavelengths, so a single wavelength of excitation light allows quantum dots to multiply. Application and feature s: Currently, water-soluble quantum dots and oil-soluble quantum dots can be coupled with molecules such as antibodies and streptavidin, and are used in biomarker detection, high-throughput coding, in vivo imaging, and dynamic tracing. However, the water-soluble quantum dot...

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 gre...