Resources

Proteomics Databases



Metabolomics Databases

• • Procedure for Protein Identification Using Tandem MS

  Proteins are fundamental molecular units of life, and understanding their structure and function is crucial for biological research. Mass spectrometry (MS) is an efficient analytical tool widely used in proteomics. Specifically, tandem mass spectrometry (MS/MS) provides detailed information about proteins and their peptides, significantly advancing the process of protein identification. This article details the procedure of protein identification using tandem mass spectrometry.

• • Mechanism of N-Glycan Relative Quantification via 2-AA Labeling

  N-glycosylation is a fundamental post-translational modification in eukaryotes and some prokaryotes, involved in key biological processes such as protein folding, stability, cell signaling, and immune response. To better understand the variation of N-glycans under different conditions, relative quantification techniques are essential. 2-Aminobenzoic acid (2-AA) labeling is a widely used method for this purpose.

• • Protein Characterization Based on WB

  Proteins are among the most crucial biomolecules in living organisms, responsible for executing various key functions. To understand protein functions, structures, and their roles in biological processes, researchers have developed various techniques for protein characterization. Among these, Western Blotting is a widely used and powerful technique.

• • Application of MALDI-TOF/LC-MS in N-Glycan Type Detection

  Glycosylation, a widespread post-translational modification (PTM) in eukaryotic proteins, plays a crucial role in protein function, stability, and cell communication. Among the various types of glycosylation, N-glycosylation is particularly important. Studying N-glycan structures and types is essential for understanding diseases such as cancer and autoimmune disorders, as well as for developing biomarkers.

• • Workflow of N-Glycan Profiling by PNGase F Digestion and 2-AA Labeling

  N-glycan profiling is a widely used technique in biological research and clinical applications to elucidate glycosylation patterns of glycoproteins. This method is crucial for understanding cellular processes, disease mechanisms, and the discovery of biomarkers. By digesting glycoproteins with PNGase F (Peptide-N-Glycosidase F) to release N-glycans and labeling them with 2-AA (2-Aminobenzoic acid), researchers can effectively analyze glycan structures.

• • Advantages and Disadvantages of Glycan Profiling Using MALDI-TOF/LC-MS

  Glycan profiling is a crucial step in understanding the structure and function of glycans. In recent years, mass spectrometry-based analytical techniques such as MALDI-TOF (Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry) and LC-MS (Liquid Chromatography-Mass Spectrometry) have played a pivotal role in glycan analysis. These technologies provide high sensitivity and throughput for glycan analysis, but each has its own advantages and limitations.

• • Mechanism of Glycan Release in Glycosylation Site Detection Using 18O Labeling

  Glycosylation is a crucial form of post-translational modification in proteins, widely present in cell surface and secreted proteins. Understanding glycosylation is vital for elucidating protein function, cellular signaling, and disease progression. One of the primary focuses of glycosylation research is the site-specific identification of glycan-modified locations.

• • Principle of Glycan Profile Analysis Based on MALDI-TOF/LC-MS

  Glycan profiling is a crucial bioanalytical technique extensively used in biomedical research, particularly in the study of protein glycosylation. Glycosylation, an essential post-translational modification, significantly impacts protein structure, function, and biological behavior.

• • Application of Glycosylation Site Analysis in Protein Function Studies

  Glycosylation is one of the most common and complex forms of post-translational modifications (PTMs) and is widely found in mammals, plants, and microorganisms. By attaching sugar moieties to specific amino acid side chains, glycosylation modulates protein functions such as stability, activity, localization, and interactions with other molecules.

• • Workflow of Glycosylation Site Identification via Enzymatic Digestion and LC-MS/MS

  Glycosylation is a specific type of post-translational modification of proteins, playing a crucial role in numerous biological processes such as cell signaling, protein folding, and immune responses. Identifying the exact glycosylation sites on proteins is critical for advancing our understanding of these processes. Enzymatic digestion combined with LC-MS/MS (liquid chromatography-tandem mass spectrometry) is currently one of the most widely used methods for glycosylation site identification.