Resources

Proteomics Databases



Metabolomics Databases

• • How to Analyze Protein Isoelectric Points?

  What is the isoelectric point of a protein? The isoelectric point of a protein refers to the pH value at which the protein exhibits a neutral charge in a solution. When the isoelectric point of a protein is equal to the pH value of the solution, the protein carries no positive or negative charge. The isoelectric point of a protein has important implications for its solubility, stability, and functionality.

• • Choosing Protein Purity Detection Methods: Comparing HPLC With MS

  Protein is an important functional molecule in organisms, and the purity of protein directly affects the results of drug development and biological research. Therefore, accurate and rapid detection of protein purity has become an important task for researchers and pharmaceutical companies.

• • New Advances in Protein Purity: Exploring CO-IP-MS Benefits and Applications

  Protein is an important functional molecule in organisms, and its purity is of great significance for research and application. Traditional protein purity analysis methods have some limitations, but in recent years, a new technology called co-immunoprecipitation-mass spectrometry (CO-IP-MS) has made breakthroughs in the field of protein purity analysis.

• • Application of New Technology for Protein N-Terminal Sequencing: IP and CO-IP

  Introduction Proteins are important functional molecules in living organisms, and studying their structure and function is crucial for understanding biological processes and disease mechanisms. Protein sequencing from scratch is a commonly used technique that can help us understand the composition and interaction relationships of proteins.

• • Comprehensive Guide to Protein Purity Detection: CO-IP and MS Applications Analysis

  Protein is an important functional molecule in organisms, and its purity is crucial for research and application. Protein purity detection is the process of determining the content and purity of the target protein in a protein sample.

• • New Advances in Protein Interaction MS: HPLC Detection Prospects

  Proteins are one of the most important functional molecules in organisms, and they form complex networks through interactions with each other, participating in the regulation of cellular physiological processes. Understanding the interactions between proteins is of great significance for revealing cellular functions and disease mechanisms. Protein-protein interaction mass spectrometry analysis is an effective method that can help us study the network of protein interactions.

• • Protein Modification Proteomics

  Post-translational modifications proteomics (PTM proteomics) is a systematic analysis method for studying post-translational modifications (PTMs) in proteins. PTMs are significant biochemical events within cells and play key roles in almost all biological processes, including signal transduction, cell cycle regulation, gene expression, and cell death, etc.

• • Common Methods of Protein Phosphorylation Modifications Detection

  Protein phosphorylation modification is a key event in cellular signal transduction, therefore accurate detection and quantification of it are essential. The commonly used methods for detecting protein phosphorylation modification mainly include:   1. Western Blot Use antibodies specific to the phosphorylation site to detect phosphorylated proteins. This method can provide semi-quantitative data for specific phosphorylation sites.

• • Protein In Vitro Phosphorylation Detection

  Protein phosphorylation is one of the most important post-translational modifications in organisms, involved in many life processes such as the cell cycle, signal transduction, and metabolic regulation. Protein in vitro phosphorylation detection, as an experimental technique, is crucial for our in-depth understanding of protein function and related disease mechanisms.

• • Ubiquitin Protein and Ubiquitination

  Ubiquitin Protein Ubiquitin is a small, highly conserved protein, composed of approximately 76 amino acids. It is present in all eukaryotic organisms and is involved in many cellular processes.   Ubiquitination Ubiquitination is a post-translational modification process in which ubiquitin forms a covalent bond with a specific amino acid residue (usually lysine) of the target protein through its C-terminus.