Resources

Proteomics Databases



Metabolomics Databases

• • Analysis of C-Terminal Sequencing Using LC-MS/MS

  C-terminal sequencing plays a crucial role in proteomics research. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) is a powerful tool for identifying C-terminal sequences.

• • Sequence Analysis of Proteins Using Multi-Enzyme Digestion Coupled with LC-MS/MS

  Proteins are crucial in executing biological functions, and understanding their structure and function is essential for elucidating biological phenomena. Traditional methods like Edman degradation provide some sequence information but are inefficient and lack sensitivity, making them unsuitable for complex protein samples. LC-MS/MS combines the separation capabilities of liquid chromatography with the detection power of mass spectrometry, establishing itself as a critical tool in modern proteomics research.

• • Detection of Protein-Protein Interactions by Co-Immunoprecipitation

  Protein-protein interactions (PPIs) are crucial in regulating various cellular processes. Understanding these interactions is key to revealing fundamental cellular mechanisms and identifying potential targets for new therapies. Co-Immunoprecipitation (Co-IP) is a classical and widely adopted technique that enables the study of protein complexes and interactions in conditions that closely mimic the physiological environment.

• • Detection of Antibody Modifications by De Novo Sequencing

  Antibodies are essential in biomedical research and clinical treatment, particularly for disease diagnosis and therapy. Modifications of antibodies, such as glycosylation and phosphorylation, significantly impact their function and stability. Therefore, accurately detecting and identifying these modifications is crucial for understanding their biological roles and optimizing their applications.

• • Mechanism of Label-Free Quantitative Proteomics

  Label-free quantitative proteomics (LFQ) is a method used to measure the relative abundance of proteins in different biological samples using mass spectrometry (MS). By comparing the intensities of signals generated by peptides, LFQ provides a high-throughput, accurate, and label-free way to quantify proteins. This makes it a highly valuable tool in large-scale studies such as protein interaction analysis, biomarker discovery, and drug target screening.

• • Advantages and Disadvantages of Label-Free Quantitative Proteomics

  Label-free quantitative proteomics (LFQ) is a powerful tool in protein research, enabling direct analysis of unlabeled protein samples through mass spectrometry, with relative quantification based on signal intensity. Compared to traditional labeling methods, LFQ presents several advantages in specific experimental scenarios but also comes with limitations.

• • Application of Label-Free Quantitative Proteomics

  Label-Free Quantitative Proteomics (LFQ) is a powerful method used for the relative quantification of proteins across different biological samples. By employing mass spectrometry (MS), LFQ avoids the complexity of chemical labeling, instead relying on the measurement of peptide ion intensities for protein quantification. Its ease of use and compatibility with high-throughput workflows have made it a crucial tool in diverse fields, including biomedicine, drug discovery, and biomarker identification.

• • Principle of Label-Free Quantitative Proteomics

  Proteomics is an essential tool for comprehensively studying protein expression and function within biological systems. Label-free quantitative proteomics is a technique that measures protein abundance directly through mass spectrometry (MS), eliminating the need for stable isotope labeling or chemical tags. This method is gaining prominence in proteomics research due to its simplicity, flexibility, and reduced sample requirements compared to other quantitative approaches.

• • Application of Quantitative Acetylproteomics

  As research into post-translational modifications (PTMs) progresses, acetylation has been identified as a pivotal modification that plays an essential role in regulating cellular function, signal transduction, and metabolism. Quantitative acetyl-proteomics, through the integration of mass spectrometry and proteomic analysis, provides a robust framework for comprehensively and quantitatively assessing the impact of acetylation in various biological processes.

• • Mechanism of Quantitative Acetylproteomics

  Acetylation is a common post-translational modification (PTM) involving the addition of an acetyl group to lysine residues of proteins. This modification plays a crucial role in various cellular processes, including cell cycle regulation, gene expression control, and metabolic regulation. To gain a deeper understanding of the functional roles of protein acetylation, quantitative acetyl-proteomics techniques have been widely employed.