Resources

Proteomics Databases



Metabolomics Databases

• • O-Glycosylation and Modification Site Analysis in Bone Tissue

  Bone tissue, as the hardest tissue in the human body, plays important roles in supporting body weight and protecting internal organs. However, the health and stability of bone tissue are not only dependent on its mineralization degree and density, but also on the complex interactions of various biomolecules in bone cells. Among them, protein glycosylation is a key process.

• • Mechanism of Pull-Down Coupled with MS for Protein Identification

  Protein pull-down combined with mass spectrometry (MS) is a pivotal technique for investigating protein-protein interactions. This method allows for the specific capture of a target protein and its interacting partners, followed by MS analysis, ultimately identifying the group of proteins that directly or indirectly interact with the target protein. Below is a detailed explanation of the mechanisms underlying protein pull-down and MS identification.

• • Application of Pull-Down Coupled with MS for Protein Identification

  Proteins play critical roles in living organisms, executing various functions in cellular signaling, metabolic regulation, and gene expression. Protein-protein interactions are fundamental to these processes and are closely tied to many diseases' onset and progression. Studying these interactions is therefore vital for understanding biological processes and developing innovative therapies.

• • Workflow of Pull-Down Coupled with MS for Protein Identification

  Protein pull-down assays combined with mass spectrometry (MS) analysis are powerful techniques for investigating protein-protein interactions. By purifying and identifying proteins that interact with a target protein, this method offers invaluable insights into the functions of proteins and the biological processes they participate in. Below is a detailed description of the workflow involved in protein pull-down and mass spectrometry identification.

• • Advantages and Disadvantages of Pull-Down Coupled with MS for Protein Identification

  Protein pull-down coupled with mass spectrometry (MS) is a widely employed technique in studying protein-protein interactions, particularly in biochemistry and molecular biology. This method uses tagged fusion proteins, specific antibodies, or biotinylated ligands to capture target proteins, followed by their identification and analysis using MS. It helps researchers identify interacting partner proteins and provides quantitative data on these interactions.

• • Principle of Pull-Down Coupled with MS for Protein Identification

  Protein pull-down technology is a classical biochemical method commonly used to study protein-protein interactions. When combined with mass spectrometry (MS) analysis, pull-down technology can effectively identify and confirm interacting partners within protein complexes.

• • Application of Pull-Down and MS in Fusion Protein Interaction Analysis

  Fusion protein technology is an essential tool in the study of protein interactions and has seen extensive application in molecular biology. By fusing a target protein with an easily detectable tag, researchers can streamline the processes of purification, detection, and functional analysis.

• • Mechanism of Pull-Down and MS in Fusion Protein Interaction Analysis

  Fusion protein interaction analysis is a fundamental tool in modern molecular biology research. By investigating protein-protein interactions, we can gain a deeper understanding of protein functions, signaling pathways, and various physiological activities within cells. The combination of Pull-Down assays and Mass Spectrometry (MS) has emerged as a highly effective approach for examining these interactions.

• • Workflow of Pull-Down and MS in Fusion Protein Interaction Analysis

  Fusion protein technology is a widely utilized method for studying protein-protein interactions. By creating a fusion between a target protein and a tag protein that is easy to detect or purify, researchers can effectively capture and identify interacting proteins. The integration of Pull-Down assays with mass spectrometry enables precise identification and quantitative analysis of these interactions.

• • Advantages and Disadvantages of Pull-Down and MS in Fusion Protein Interaction Analysis

  Protein-protein interactions (PPIs) are critical to various biological processes, such as signal transduction, metabolic regulation, and cellular structure maintenance. Understanding these interactions is essential for elucidating the underlying mechanisms of cellular functions. Among the numerous methods developed for studying PPIs, fusion protein interaction analysis based on Pull-Down assays and mass spectrometry has become a widely adopted technique.