Resources

Proteomics Databases



Metabolomics Databases

• • Workflow of DIA-PRM Proteomics

  Data-Independent Acquisition - Parallel Reaction Monitoring (DIA-PRM) is a proteomics analysis method that combines the strengths of Data-Independent Acquisition (DIA) and Parallel Reaction Monitoring (PRM) mass spectrometry techniques. DIA enables the acquisition of spectral data from all analytes in a sample within a single run, while PRM allows for high-precision, quantitative analysis of specific target peptides during subsequent analyses.

• • Principle of DIA-PRM Proteomics

  DIA (Data-Independent Acquisition) and PRM (Parallel Reaction Monitoring) are two critical mass spectrometry techniques in the field of proteomics. As scientific research progresses, proteomics methods continue to evolve, making protein quantification and identification more accurate and efficient.

• • Mechanism of Semi-Quantitative Proteomic Analysis

  Semi-quantitative proteomics analysis is a technique used to study changes in protein expression levels by comparing the relative abundance of proteins under different experimental conditions, thereby revealing underlying biological mechanisms. Unlike quantitative proteomics, semi-quantitative analysis does not rely on absolute quantification but instead infers trends by comparing the relative abundance of proteins across multiple samples.

• • Application of Semi-Quantitative Proteomic Analysis

  Proteomics is the study of the structure, function, and interactions of all proteins in a biological system. Recent advancements in proteomics research have been driven by significant improvements in mass spectrometry (MS) technology and the development of bioinformatics tools. Semi-quantitative proteomics analysis, a key research technique, has attracted attention for its ability to provide relative protein abundance information without requiring absolute quantification standards.

• • Workflow of Semi-Quantitative Proteomic Analysis

  Semi-quantitative proteomics is a widely used technique in biomedical research, enabling the identification and relative quantification of proteins within complex biological samples using mass spectrometry. Unlike fully quantitative proteomics, semi-quantitative analysis focuses on comparing changes in protein abundance under different conditions, providing insights into the dynamic changes occurring in biological systems.

• • Principle of Semi-Quantitative Proteomic Analysis

  As proteomics research progresses, there is an increasing demand for quantitative analysis of protein expression levels. Semi-quantitative proteomics analysis offers an efficient and cost-effective approach to estimating the relative abundance of proteins.

• • Protein Mass Spectrometry: Comprehensive Comparison of Methods for Peptide Purity Detection

  Proteins are vital components of living organisms and are vital in the study of biological functions and drug development. As the building blocks of proteins, the purity detection of peptides is crucial for ensuring the accuracy of experimental results and the safety of drugs.

• • How Does the Order of Protein Mass Spectrometry Injection Affect the Identification of Peptide Structures?

  Proteins are one of the most important molecules in biological organisms, playing a key role in cellular functions and biological processes. Understanding the structure and function of proteins is of great significance in the study of biology and the development of biopharmaceuticals. Proteomic mass spectrometry is a common technique used to identify protein sequences and structures.

• • Quantification of Free Sulfhydryl Groups in Recombinant Protein Vaccines

  Recombinant protein vaccines are prepared using genetic engineering technology, with the aim of eliciting an immune response by expressing and producing specific proteins of pathogens. These vaccines do not contain complete active pathogens but select specific proteins or parts of the pathogens as antigens. In the structure of proteins, mercapto mainly exists in cysteine, playing a key role in protein folding and stability.

• • Mechanism of 2D-DIGE-Based Protein Quantification

  In proteomics research, accurate protein quantification is a fundamental task. Traditional protein quantification methods, such as one-dimensional polyacrylamide gel electrophoresis (1D-PAGE), often face limitations in resolution and sensitivity, making it difficult to distinguish and quantify proteins in complex samples precisely.