Resources

Proteomics Databases



Metabolomics Databases

• • Application of Mass Spectrometry in O-Glycan Site Analysis

  O-glycosylation is a significant form of post-translational modification of proteins, prevalent in membrane proteins, secreted proteins, and their derivatives. O-glycosylation plays a crucial role in various biological processes, including cell signaling, immune responses, and cell recognition. Therefore, quantitative analysis of O-glycosylation sites is vital for understanding their biological functions.

• • Principle of O-Glycan Modification and Site Identification

  O-glycosylation is the process by which sugar chains are added to serine (Ser) or threonine (Thr) residues on proteins through glycosylation reactions. This modification significantly influences protein function, stability, and cellular signaling. Understanding the principles of O-glycosylation and methods for site identification is thus crucial for biological research and its applications.

• • Mechanism of O-Glycosylation and Its Impact on Biological Products

  O-glycosylation refers to the process where sugar molecules bind to the hydroxyl groups of amino acids through ester or ether bonds, forming O-glycosidic bonds. This modification plays a vital role in numerous biological processes within organisms, affecting the functionality and stability of proteins.

• • Application of O-Glycosylation Site Analysis in Biological Products

  O-glycosylation is a crucial form of post-translational modification of proteins, widely present in various organisms, especially in bioproducts. This modification not only affects the structure and function of proteins but also closely relates to many physiological and pathological processes in organisms. Therefore, analyzing O-glycosylation sites in bioproducts can provide important information regarding their biological functions and potential applications.

• • Workflow of O-Glycosylation Site Analysis in Biological Products

  O-glycosylation is an important post-translational modification that is widely present in various biological proteins, particularly in bioproducts. It plays a critical role in protein function, stability, and intercellular interactions. Therefore, studying the workflow for analyzing O-glycosylation sites is crucial for quality control and functional research of bioproducts.

• • Protein Identification Guide: Comprehensive Analysis of IP and Co-IP Gel Spots

  Proteins are important functional molecules in organisms, and they are significant in studying biological processes and disease mechanisms. Protein identification is one of the key steps in studying protein interactions and functions.

• • Principle of O-Glycosylation Site Analysis in Biological Products

  O-glycosylation is a significant post-translational modification involving the addition of sugar molecules to serine or threonine residues, crucial for biological functions such as protein stability, functionality, and intercellular interactions. This analysis has become a key focus in understanding protein functions and disease mechanisms in modern biotechnology.

• • Personalized Cancer Treatment: Immuno-Peptidomics and MS Reveal the Secrets of Tumor Neoantigens

  Immunopeptidomics research focuses on exploring all peptides related to the antigen presentation process. These peptides play a crucial role in both cell-mediated and humoral immune responses. Immunopeptidome refers to the study of the complete set of peptides presented by MHC class I or II molecules on nucleated cells involved in antigen presentation pathways. They are essential for investigating immunogenic epitopes involved in cell-mediated and humoral immune responses.

• • X-Ray Powder Diffraction Analysis of Peptide Drug

  Peptide drugs are biologically active molecules composed of multiple amino acids linked by peptide bonds. Typically, they consist of 10 to 100 amino acids with a relative molecular weight below 10,000. Most peptide drugs originate from endogenous or natural peptides, thus they have little to no side effects on the human body. Compared to protein drugs, peptide drugs also offer advantages such as good stability, high purity, low production costs, and low immunogenicity.

• • Inactivated Vaccine Viral Inactivant Residue Testing

  Inactivated vaccines are vaccines that are made by culturing and then inactivating the pathogenic microorganisms. They are a common type of vaccine. By culturing and inactivating bacteria, viruses, or rickettsiae, the vaccines lose their pathogenicity to target organs while preserving the immunogenicity of the antigens. They can stimulate the immune system to produce an immune response, thereby achieving the purpose of disease prevention and treatment.