Resources

Proteomics Databases



Metabolomics Databases

• • Advantages and Disadvantages of HILIC-UHPLC in N-Glycan Detection

  In biochemical and glycomic research, the analysis of N-linked glycans (N-glycans) is crucial. The structure and function of N-glycans significantly impact physiological processes in living organisms, making the development of efficient and sensitive analytical methods essential. In recent years, Hydrophilic Interaction Liquid Chromatography-Ultra High Performance Liquid Chromatography (HILIC-UHPLC) has emerged as a promising separation technique for N-glycan detection, showcasing unique advantages.

• • Principle of HILIC-UHPLC in N-Glycosidic Bonds Analysis

  With the deepening of research into glycoscience, the analysis of N-glycans has garnered increasing attention in the fields of biomedicine, drug development, and biotechnology. N-glycans, as modifications of glycan chains, are widely present in various proteins and lipids, and changes in their structure are closely related to multiple diseases, such as cancer and diabetes. Therefore, developing efficient analytical methods is crucial for uncovering their biological functions and related mechanisms.

• • Mechanism of O-Glycan Profiling

  O-glycans are carbohydrate chains formed through glycosylation reactions with hydroxyl amino acid residues, widely present in various proteins, especially in membrane and secreted proteins. Analyzing O-glycans is crucial for understanding their biological functions, structural characteristics, and roles in diseases.

• • Application of O-Glycan Profiling

  O-glycans are a crucial type of carbohydrate involved in various biological processes, including cell signaling, protein functionality, and stability. Therefore, the analysis of O-glycans is vital for biological research and medical diagnostics.

• • Workflow of O-Glycan Profiling

  O-glycans are polysaccharides formed by the attachment of sugar molecules to proteins or lipids via oxygen bonds. They are widely present in biological systems and play critical roles in biological functions and disease mechanisms. Analyzing O-glycans is essential for understanding their involvement in cellular signaling, immune responses, and cell recognition.

• • Principle of O-Glycan Profiling

  O-glycans are carbohydrate modifications of proteins or peptides, formed through linkage to the hydroxyl groups of serine or threonine residues. These modifications play significant roles in physiological functions, including signal transduction, intercellular interactions, and immune responses. Therefore, the analysis of O-glycans is vital for understanding their functions in biological processes.

• • Amino Acid Chirality Analysis of Peptide Drugs (LC-MS)

  Peptide drugs are biologically active molecules composed of multiple amino acids linked by peptide bonds. Typically, they consist of 10 to 100 amino acids with a molecular weight below 10,000. Peptide drugs are mostly derived from endogenous or natural peptides, thus they have little or no side effects on the human body. Compared to protein-based drugs, peptide drugs have advantages such as good stability, high purity, low production costs, and low immunogenicity.

• • Mass Spectrometry for Molecular Weight: Common Methods and Applications

  Mass spectrometry molecular weight determination is one of the commonly used analytical techniques in the field of biopharmaceutical research. By measuring the mass of molecules, scientists can understand the structure and properties of molecules, thereby advancing drug development and biological research.

• • Exploring Peptide Mapping Analysis: Unraveling Protein Composition Diversity

  Peptide mapping analysis is a method used to analyze the diversity of protein composition. This article will provide a detailed introduction to the principles and applications of peptide mapping analysis. Protein Composition Diversity Proteins are composed of amino acids, and the types and sequences of amino acids determine the structure and function of proteins. In living organisms, the same protein may exist in multiple different forms, which is known as protein composition diversity.

• • Protein Interaction Analysis by Mass Spectrometry

  Protein-protein interaction mass spectrometry analysis is an important technique for studying the interactions between proteins. It utilizes mass spectrometry to determine the structure and properties of protein molecules by measuring their mass and charge. Protein-protein interaction mass spectrometry analysis, on the other hand, involves analyzing the interactions between proteins to uncover their functions and regulatory mechanisms within cells.