Resources

Proteomics Databases



Metabolomics Databases

• • Workflow of Quantitative Ubiquitinomics

  Ubiquitination is a widely conserved post-translational modification in eukaryotes, where small ubiquitin proteins are covalently attached to target proteins, regulating various cellular processes. This modification plays a pivotal role in protein degradation, signal transduction, and DNA repair. With advancements in mass spectrometry (MS) technologies, quantitative ubiquitinomics has emerged as a crucial tool for uncovering the molecular mechanisms and dynamic changes of ubiquitination in cellular systems.

• • Mechanism of Phosphoprotein Enrichment in Phosphoproteomics

  Phosphorylation is a prevalent post-translational modification of proteins, significantly impacting various biological processes such as signal transduction, cell cycle regulation, and metabolism. The study of phosphoproteomics is therefore critical for understanding cellular functions and disease mechanisms.

• • Principle of Quantitative Ubiquitinomics

  Ubiquitination is a crucial post-translational modification, where ubiquitin molecules covalently attach to proteins, regulating their function, localization, and degradation. As mass spectrometry and proteomics technologies advance, quantitative ubiquitomics has emerged as a powerful tool for studying the ubiquitination state of proteins.

• • Application of Quantitative Phosphoproteomics in Cellular Signaling

  Cell signal transduction is a vital process that allows cells to perceive and respond to external stimuli, orchestrating a complex network of biochemical reactions. Phosphorylation, a prevalent post-translational modification, plays a crucial regulatory role in cell signaling.

• • Workflow of Quantitative Phosphoproteomics

  Quantitative phosphoproteomics is a powerful tool for studying the phosphorylation status of proteins and their roles in cellular signaling and metabolism. Phosphorylation, as a common post-translational modification, is crucial for regulating cellular functions. Therefore, understanding its dynamic changes is essential for elucidating disease mechanisms and developing therapeutic strategies.

• • Deamidation Detection of Protein Post-Translational Modification

  Post-translational modification (PTM) refers to the chemical modifications that occur after protein translation. These modifications can influence the activity, stability, affinity, half-life, and intracellular localization of the protein.   Deamidation is a form of PTM where the protein loses an amide group (usually by removing the amide group on the amino acid side chain) after translation.

• • 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.