Resources

Proteomics Databases



Metabolomics Databases

• • Key Methods for Protein Sequence Analysis: Deciphering the Fundamental Composition of Biomolecules

  Protein Sequence Determination Methods Protein sequence determination is the foundation of protein sequence analysis. The commonly used protein sequence determination methods include: 1. Sanger Sequencing Sanger sequencing is a classic sequencing method, which determines the amino acids in the protein sequence one by one through DNA synthesis reaction. This method is highly accurate and reliable, but the sequencing speed is relatively slow, suitable for small-scale protein sequence determination.

• • Mechanism of DIA-PRM Proteomics

  The development of proteomics technology has provided powerful tools for understanding protein functions, interactions, and regulatory mechanisms within cells. Among the various proteomics techniques, Data-Independent Acquisition (DIA) and Parallel Reaction Monitoring (PRM) have become increasingly favored by researchers. By combining the strengths of both methods, DIA-PRM has emerged as a powerful technique for high-throughput and highly sensitive protein quantification.

• • Application of DIA-PRM Proteomics

  DIA (Data-Independent Acquisition) and PRM (Parallel Reaction Monitoring) are two mass spectrometry techniques widely used in proteomics research. DIA’s primary feature is its ability to scan all peptides simultaneously, providing comprehensive quantitative data. PRM, in contrast, selectively monitors target peptides, achieving higher quantification accuracy.

• • Advantages and Disadvantages of DIA-PRM Proteomics

  Data-Independent Acquisition (DIA) and Parallel Reaction Monitoring (PRM) are two mass spectrometry techniques that have gained considerable attention in proteomics research. DIA captures all precursor ions and their fragment spectra in an unbiased manner, ensuring comprehensive data acquisition, while PRM targets specific precursor ions and their fragment ions, providing high specificity and quantitative accuracy.

• • 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.