Resources

Proteomics Databases



Metabolomics Databases

• • Detection of Protein Modifications by Top-Down Sequencing

  Proteins are the primary agents of life activities, performing a wide range of functions such as catalyzing biochemical reactions, providing structural support, and transmitting signals. The functionality of a protein is determined not only by its amino acid sequence but also by its post-translational modifications (PTMs). PTMs refer to the chemical alterations that occur after protein synthesis, modifying its properties and functions.

• • Procedure for Peptide Sequencing Based on De Novo Method

  In proteomics research, peptide sequencing is a crucial technique for understanding protein structure and function. Unlike traditional database search methods, De Novo sequencing does not rely on known protein sequence databases but directly derives amino acid sequences from mass spectrometry data.

• • Analysis of Top-Down Protein Sequencing by MALDI ISD

  Proteins are essential functional molecules within organisms, and studying their structure and function is crucial for understanding life processes. The development of protein sequencing technologies provides powerful tools for revealing the amino acid sequences and structures of proteins. Among these technologies, Matrix-Assisted Laser Desorption/Ionization (MALDI) combined with In-Source Decay (ISD) has emerged as an efficient and precise method for top-down protein sequencing.

• • Analysis of Peptide Sequencing Using Mass Spectrometry

  In biological research, analyzing protein structures and functions is critical to understanding biological system mechanisms. Peptides, the fundamental units of proteins, provide vital sequence information necessary for elucidating protein structure and function. Mass spectrometry, known for its high sensitivity and resolution, has become an essential tool for peptide sequencing analysis.

• • Analysis of N-Terminal Sequencing Using Edman Degradation and Mass Spectrometry

  N-terminal sequencing is a critical technique in protein analysis, primarily used to determine the amino acid sequence at the N-terminus of a protein or peptide. This method is essential in characterizing protein structures, identifying proteins, and understanding their functional properties. 

• • 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.