Resources

• • Mechanism of Chemical Proteomics Analysis

  Chemical proteomics is a research approach that combines chemical tools with mass spectrometry to study protein function, interactions, and modification states. The central mechanism involves using chemical probes, reactive compounds, or labeling molecules to identify proteins or their modification sites, followed by qualitative and quantitative analysis using mass spectrometry.

• • Application of Chemical Proteomics Analysis

  Chemical proteomics, a technique that utilizes chemical probes and targeted reactions to detect and functionally analyze proteome components, has found broad applications in the biomedical field. With advancements in analytical techniques, chemical proteomics has become a powerful tool for biological research and drug development. Its application spans from target identification to biomarker discovery, advancing research in precision medicine and drug development.

• • Principle of Chemical Proteomics Analysis

  Chemical proteomics is an emerging field that leverages the interaction between chemical probes and proteins to study protein function, structure, and activity within the cellular environment. By integrating chemical synthesis with proteomics techniques, it allows the identification, quantification, and functional analysis of proteins through specific chemical modifications or labeling.

• • Workflow of Chemical Proteomics Analysis

  Chemical proteomics is a technique that utilizes chemical methods to label, capture, or modify proteins in order to study their structure and function. This analytical technology has broad applications in drug discovery, biomarker identification, and protein function research. The workflow of chemical proteomics analysis typically involves several key steps, each of which is crucial for the success of the experiment. Below is a detailed description of the workflow of chemical proteomics analysis.

• • Mechanism of AQUA in Protein Detection

  Absolute Quantification of proteins (AQUA) is a key technology in proteomics, utilizing stable isotope-labeled peptides for precise protein quantification. Combined with mass spectrometry (MS), AQUA enables the absolute quantification of target proteins, providing crucial insights into biomarker discovery, drug target validation, and functional analysis of proteins.

• • Workflow of AQUA in Quantitative Proteomics

  AQUA (Absolute Quantification) is an isotope-labeled mass spectrometry-based technique used for the precise absolute quantification of specific peptides from target proteins. By incorporating known amounts of synthetic peptides as internal standards, AQUA provides absolute quantification of target peptides in a sample. The workflow of AQUA involves multiple critical steps, ranging from sample preparation to data processing and analysis, which ensures accuracy and reproducibility.

• • Advantages and Disadvantages of AQUA Technique

  Absolute quantification analysis (AQUA) is a mass spectrometry-based technique used for the absolute quantification of proteins. It has become a vital tool in proteomics research. By using isotopically labeled peptides as internal standards, AQUA allows for precise quantification of proteins and peptides. Due to its high sensitivity, specificity, and accuracy, AQUA technology has been widely adopted in fields such as biomedicine, drug discovery, and basic life sciences.

• • Principle of Absolute Quantitative Analysis

  In proteomics research, quantitative analysis is essential for understanding the changes in protein expression levels under different biological conditions. Absolute Quantification (AQUA) is a precise and reliable method widely used in proteomics for accurate quantification. The AQUA technique relies on mass spectrometry (MS) and isotopically labeled standards to measure the amount of target proteins or peptides in an absolute manner.

• • Detection of N-Glycan Types in Glycosylated Proteins Based on LC-MS

  Glycosylation is a significant post-translational modification process in living organisms, critically influencing the function, stability, and intercellular interactions of proteins. N-glycosylation, a specific form of glycosylation, typically occurs on the asparagine residues of proteins. The types and structures of N-glycans can vary among different organisms and cellular states, impacting biological functions and pathological conditions.

• • Steps of Glycosylation Site Analysis Using LC-MS/MS

  Glycosylation is a crucial post-translational modification that profoundly impacts the structure and function of proteins. Identifying glycosylation sites is essential for understanding the roles of biomolecules within cells and their potential mechanisms in diseases. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) has emerged as an efficient analytical tool widely used in glycosylation site research.