Resources

Proteomics Databases



Metabolomics Databases

• • Application of MALDI-TOF-MS in N-Glycan Profiling

  N-glycans are polysaccharides attached to proteins through glycosylation modifications, prevalent in biological systems. They play critical roles in biological processes, including cell signaling, immune responses, and cell recognition. As research in glycobiology progresses, the demand for efficient N-glycan analysis has surged.

• • Workflow of N-Glycan Profiling for Structural Analysis

  N-glycans, polysaccharides attached to proteins via glycosylation, have complex structures and essential functions. Understanding the structure of N-glycans is crucial for elucidating their biological roles.

• • Advantages and Disadvantages of N-Glycan Profiling Using HILIC-UHPLC-MS

  N-glycans are polysaccharides attached to proteins through glycosylation modifications, widely present in living organisms. They play crucial roles in biological processes such as cell signaling, immune responses, and cell recognition. As research in glycobiology deepens, the demand for efficient analysis of N-glycans has increased.

• • Principle of N-Glycan Profiling Based on MALDI-TOF-MS

  Glycosylation refers to the process of carbohydrates binding to proteins, lipids, or other biomolecules, playing a crucial role in cellular signaling, immune responses, and protein stability. N-glycosylation, a major form of glycosylation, involves oligosaccharide chains attached to amino acid residues. In recent years, N-glycan analysis based on Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF-MS) has become a focus of attention for researchers.

• • Mechanism of Glycosylation Site and Glycoform Analysis

  Glycosylation refers to the attachment of carbohydrate molecules to proteins or lipids, serving as a crucial form of post-translational modification. The identification of glycosylation sites and the analysis of glycans are vital for understanding various biological functions and play significant roles in disease diagnosis and treatment. Glycosylation is mainly categorized into N-glycosylation, which occurs on asparagine or lysine residues, and O-glycosylation, which occurs on serine or threonine residues.

• • Application of Glycosylation Site and Glycoform Analysis

  Glycosylation is an essential post-translational modification that significantly influences cellular functions and overall health. The analysis of glycosylation sites and glycan structures is critical in biomedical research, drug development, and fundamental biological studies.

• • Workflow of Glycosylation Site and Glycoform Analysis

  Glycosylation refers to the process of sugar molecules attaching to proteins, lipids, and other biomolecules. This process significantly impacts the functions, structures, and interactions of biological entities. The study of glycosylation sites and glycan analysis helps us understand the complexities of these biological processes.

• • Principle of Glycosylation Site and Glycoform Analysis

  Glycosylation refers to the process of adding sugar chains to biological molecules, such as proteins and lipids. This process plays a crucial role in intercellular signaling, immune responses, cell adhesion, and protein stability. The analysis of glycosylation sites is essential for understanding cell biology and related diseases (such as cancer and diabetes).

• • Application of Quantitative Proteomics

  Quantitative proteomics is an essential tool for the quantitative analysis of proteins in biological samples using high-throughput technologies. With the rapid advancement of biotechnology, quantitative proteomics has shown extensive application potential in various fields, including disease diagnosis, drug development, and basic research.

• • Mechanism of Quantitative Proteomics

  Quantitative proteomics is a vital tool for studying protein expression levels and their changes. Utilizing high-throughput technologies, researchers can gain insights into the complex biological processes within cells.