Resources

Proteomics Databases



Metabolomics Databases

• • Mechanism of Proteomic Analysis in Complex Sample Types

  Proteomics, the comprehensive study of proteins within a biological system, has garnered significant attention in recent years, particularly in the analysis of complex sample types such as tissues, serum, and cell culture media. However, the diverse nature and varying expression levels of proteins in complex samples pose considerable challenges. Therefore, understanding the mechanisms of proteomics analysis in complex samples is crucial for researchers and application scientists alike.

• • Protein Primary Structure Determination: Decoding Linear Amino Acid Sequences

  Determining the primary structure of a protein, which involves determining the linear sequence of amino acids, is one of the fundamental aspects of molecular biology research. Since the first determination of the amino acid sequence of insulin in the 1950s, significant progress has been made in the technology.

• • Workflow of Proteomics for Different Sample Types

  Proteomics is the study of the composition, function, and interactions of proteins within a cell or organism. As technology has advanced, proteomics has become an essential tool in biological research. Different sample types, such as serum, tissues, cells, and bodily fluids, provide rich research subjects, each with unique processing and analysis workflows.

• • Mechanism of N-Glycan Modification in Cancer Diagnosis

  N-glycosylation is a protein modification process where N-acetylglucosamine (GlcNAc) is added to specific amino acid residues. This modification significantly influences the structure, stability, and function of proteins. Recent studies have highlighted N-glycosylation's critical role in cancer progression, positioning it as a valuable focus for cancer diagnosis.

• • Application of N-Glycan Modification and Site Analysis in Biomarker Discovery

  N-glycosylation is a pivotal post-translational modification that significantly influences protein function and stability. In the realm of biomarker discovery, N-glycosylation and its site analysis have become critical research focal points.

• • Workflow of N-Glycan Modification and Site Analysis

  N-glycosylation refers to the attachment of sugar chains to the nitrogen atom of amino acid residues in proteins, primarily asparagine or lysine. This modification plays a vital role in protein structure and function, influencing processes like cell signaling, immune response, and intercellular interactions.

• • Principle of N-Glycan Modification and Site Analysis

  N-glycosylation is a post-translational modification where sugar molecules attach to proteins via nitrogen atoms, specifically through asparagine residues. This modification is crucial in determining protein structure, stability, and functionality, influencing various biological processes, including cell signaling, immune response, and cellular interactions.

• • Mechanism of O-Glycan Cleavage and Methylation Analysis

  O-glycosylation refers to the addition of glycans to hydroxyl amino acid residues in proteins, an important post-translational modification that affects protein function, stability, and cellular recognition. The analysis of O-glycan cleavage and methylation is crucial for understanding the roles of O-glycosylation in biological systems.

• • Workflow of O-Glycan Site-Specific Modification Analysis

  O-glycosylation is an important post-translational modification widely present in various biomolecules, such as glycoproteins and glycolipids. It affects protein function, stability, and cell signaling, playing a crucial role in biomedical applications.

• • Application of Mass Spectrometry in O-Glycan Site Analysis

  O-glycosylation is a significant form of post-translational modification of proteins, prevalent in membrane proteins, secreted proteins, and their derivatives. O-glycosylation plays a crucial role in various biological processes, including cell signaling, immune responses, and cell recognition. Therefore, quantitative analysis of O-glycosylation sites is vital for understanding their biological functions.