Resources

Proteomics Databases



Metabolomics Databases

• • Principle of Quantitative Phosphoproteomics Analysis

  Phosphorylation is one of the most common and essential post-translational modifications (PTMs) in proteins, playing a key role in various biological processes such as cell signaling, metabolic regulation, and the cell cycle. Through quantitative phosphoproteomics analysis, scientists can accurately detect and compare phosphorylation changes under different biological conditions, thereby revealing the dynamic regulatory mechanisms of cellular signal transduction.

• • Protein Labeling Quantification

  Protein Labeling Quantification is an experimental technique used for analyzing protein expression and regulation. In the experiment, proteins are combined with specific labeling molecules, aiming to quantitatively analyze the expression levels of specific proteins or multiple proteins in different samples.   Analysis Workflow 1. Protein Extraction Proteins are first extracted from the biological samples under study (such as cells, tissues, or body fluids).

• • Unlabeled Quantification: Application of Label-Free Quantification

  In the field of biopharmaceutical research, understanding the quantitative information of proteins is crucial to understanding cellular processes and disease mechanisms. In recent years, label-free quantification has emerged, providing researchers with a more accurate and flexible method of protein quantification.

• • Unlabeled Mass Spectrometry Detection: Label-Free Proteomics Frontier

  Studying the expression levels and functional changes of proteins is of great significance for understanding biological processes and disease mechanisms. The label-free mass spectrometry detection technology has become a frontier field in proteomics research.   What Is Label-Free Mass Spectrometry Detection? Label-free mass spectrometry detection is a technique used for quantitative analysis of proteins, which does not require chemical labeling or fluorescence staining of protein samples.

• • Mechanism of Protein Oxidative Modification and Detection by Mass Spectrometry

  Protein oxidative modifications, resulting from changes in intracellular and extracellular environments, are a widespread biochemical phenomenon. Increased oxidative stress leads to the generation of reactive oxygen species (ROS), which can damage proteins by altering their structure and function. These modifications are critical in the pathogenesis of various diseases and are involved in regulating key biological processes, including cellular signaling, protein degradation, and immune responses.

• • Application of Mass Spectrometry in Protein Oxidative Modification Analysis

  Protein oxidation modifications (POMs) are prevalent molecular processes within living organisms, playing critical roles in cellular function, signal transduction, and the development of diseases. As mass spectrometry (MS) technology has advanced, it has become a pivotal tool in analyzing and identifying these modifications. The high sensitivity and resolution of MS enable the precise detection and quantification of protein oxidation modifications within complex biological samples.

• • Workflow of Protein Oxidative Modification Analysis Using Nano-LC-MS/MS

  Protein oxidation modification is a common post-translational modification associated with cellular oxidative stress. Analyzing these modifications is crucial for understanding cellular signaling pathways, metabolic regulation, and the pathophysiology of various diseases. Nano-LC-MS/MS (Nano-Liquid Chromatography coupled with Tandem Mass Spectrometry) is widely regarded as the optimal technique for analyzing protein oxidation modifications due to its superior sensitivity and resolution.

• • Principle of Protein Oxidative Modification Analysis Based on Mass Spectrometry

  Protein oxidation modification is a prevalent biochemical phenomenon that involves oxidative alterations of amino acid residues in proteins. These modifications are crucial in various biological processes, such as cellular signaling, metabolic regulation, and aging. Due to its high sensitivity and resolution, mass spectrometry (MS) has become the primary method for analyzing protein oxidation modifications.

• • Mechanism of Protein Sumoylation in Subcellular Localization

  Protein SUMOylation is a critical post-translational modification involving the covalent attachment of SUMO (Small Ubiquitin-like Modifier) to target proteins. Unlike ubiquitination, SUMOylation does not mark proteins for degradation but instead regulates their function by altering their activity, interaction partners, or subcellular localization. SUMOylated proteins are often found enriched in specific subcellular compartments, such as the nucleus, cytoplasm, or cytoskeleton.

• • Application of Protein Sumoylation Identification in Cellular Processes

  Protein SUMOylation refers to the covalent attachment of Small Ubiquitin-like Modifier (SUMO) proteins to target proteins through enzymatic reactions. This post-translational modification plays a pivotal role in regulating protein function, localization, and stability. In recent years, significant attention has been directed towards the role of SUMOylation in various cellular activities, particularly in transcriptional regulation, DNA repair, and cell cycle control.