MS Analysis Expert

Target S ample D eposition Classic Dry Liquid Droplet Method Step I: Preparation of semi-saturated cyano-4-hydroxycinnamic acid (approximately 5 mg / ml): Dissolve α-cyano-4-hydroxybenzoic acid in 300 μl of 1: 1 acetonitrile / TFA solution (ultrasonication for 10 min) .   C entrifuge  the liquid  for several seconds to obtain t he supernatant.  Add 200 μl of the supernatant to a microcentrifuge tube, and add the same volume (200 μl) of a 1: 1 acetonitrile / TFA solution t o prepare a semi-saturated α-cyano-4-hydroxycinnamic acid. Step II: Take 0.8 μl of digestion solution and 0.8 μl of matrix into a microcentrifuge tube and mix them quickly (avoid crystallization at the tip of the pipette) . Take 0.8 μl of the mixed solution onto the MALDI base . The remaining 0.8 μl of the mixed solution can be dropped on another position of the MALDI base , and the tip of the pipette should not touch the standard. Step III: Let the mixture dry naturally   and crystallize . Method

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 la

Delayed, unscheduled Alzheimer's disease accounts for 99% of all such diseases, and it is associated with a variety of pathogenic factors and pathological mechanisms. One of them is a post-translational modification  process of proteins called "O-linked beta-N acetylglucosamine modification" or "O-GlcNAc". The low content and easily decomposable properties of O-GlcNAc make it difficult to study this type of protein modification, and it is also difficult for scientists to quantitatively study O-GlcNAc on a large scale. According to an article published in the Journal of Pathology , researchers used a new approach to integrated proteomics to study this type of protein modification in detail. The author of the article is Cheng-Xin Gong from the City University of New York and Sheng Wang from the Pacific Northwest National Laboratory.   This study systematically quantified proteomic analysis of the characteristics of O-GlcNAc modification in the brain.