Resources

Proteomics Databases



Metabolomics Databases

• • Workflow of DIA in Protein Quantification

  Data-Independent Acquisition (DIA) technology is a widely used quantitative analysis method in proteomics research. Unlike the traditional Data-Dependent Acquisition (DDA), DIA technology allows for the simultaneous monitoring of all detectable peptides, thus enhancing data comprehensiveness and quantification accuracy.

• • Advantages and Disadvantages of DIA in Protein Quantification

  Data-Independent Acquisition (DIA) technology has rapidly gained popularity in proteomics research. By enabling the simultaneous collection of fragment ion data from all peptides, DIA overcomes many of the limitations associated with traditional Data-Dependent Acquisition (DDA) methods.

• • Principle of DIA in Protein Quantification

  In modern proteomics research, accurate quantitative analysis is vital for elucidating protein expression changes across various biological conditions. Data-Independent Acquisition (DIA) technology has emerged as a leading method for protein quantification due to its superior sensitivity, reproducibility, and comprehensive coverage.

• • Application of Peptide Sequencing

  Peptide sequencing is a pivotal technique for determining the amino acid sequence in proteins, offering substantial benefits across various fields such as protein structure and function analysis, disease diagnosis and treatment, drug development, biotechnology, and environmental science. Below, the diverse applications of peptide sequencing are explored in detail.

• • Mechanism of Peptide Sequencing

  Peptide sequencing is a crucial technique in protein research, allowing scientists to understand the structure and function of proteins by determining the order of amino acids in a peptide chain.

• • Workflow of Peptide Sequencing

  Peptide sequencing is an essential method for studying the structure and function of proteins. By determining the sequence of amino acids in a peptide chain, it aids scientists in understanding the biological functions of proteins and their roles within organisms. The primary steps of peptide sequencing include sample preparation, peptide generation, peptide separation, mass spectrometry analysis, data processing, and result interpretation.

• • The Principle of Peptide Sequencing

  Peptide sequencing involves determining the primary structure of a protein by analyzing the amino acid sequence of peptide fragments. Understanding the amino acid sequence of proteins is crucial for studying their function, structure, and interactions. The development of peptide sequencing technology has advanced proteomics research, enabling scientists to gain deeper insights into the mechanisms of biomolecules.

• • Advantages and Disadvantages of Peptide Sequencing

  Peptide sequencing involves determining the sequence of amino acids in a peptide chain to elucidate the structure and function of proteins. As proteomics research advances, peptide sequencing plays a crucial role in biomedical research, drug development, and disease diagnosis. However, this technology also has certain limitations in its application.

• • Antibody Drug Glycosylation Analysis

  Antibody drug glycosylation analysis is a critical bio-pharmaceutical analysis method, specifically used to evaluate and monitor the glycan structures on antibody drugs. Glycosylation analysis is crucial for ensuring the safety, efficacy, and consistency of drugs, as the structure and composition of glycans directly influence the bioactivity and pharmacokinetic properties of antibody drugs.

• • Methods for Detecting Protein Phosphorylation

  Detecting protein phosphorylation is a critical task in biological and biochemical research, as phosphorylation is one of the key processes in cell signaling. Here are some commonly used methods for detecting protein phosphorylation.   1. Immunoblotting (Western Blotting) This is one of the most common methods for detecting protein phosphorylation. It involves extracting proteins from cells or tissues and then separating them by SDS-PAGE electrophoresis.