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    Resources

      Proteomics Databases

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    • • The Structure-Function Relationship of Glycosylation Modifications

      Glycosylation is a common type of chemical modification in recombinant proteins, which is of great importance in the field of biomedicine. Glycosylation modification has a significant impact on the structure and function of recombinant proteins. As a key tool, the technology of detecting glycosylation in recombinant proteins helps us to understand the characteristics and levels of glycosylation modification and its relationship with the structure and function of recombinant proteins.

    • • Lactylation-Modified Histone Detection

      Lactylation modification is a new type of histone modification, which regulates gene expression and cell function by adding lactate groups to histones. The detection of lactylation-modified histones is a method to study lactylation modification. By revealing the association between lactylation modification and diseases, it can help us to understand the molecular mechanism of diseases and develop relevant treatments in depth.

    • • Innovative Applications Based on Chemical Proteomics

      Proteins are important molecules in organisms, playing a critical role in various life processes. The study of protein structure, function, and interaction is essential for understanding biological mechanisms and developing bio-drugs. Chemical proteomics, which combines chemistry and biology, provides new ideas and methods for protein research through the intervention of chemical means.

    • • Application of Phosphorylation Mass Spectrometry in Disease Research

      Phosphorylation is the most common and important type of protein modification. It regulates the structure, function and interactions of proteins by introducing phosphate groups into protein molecules. Phosphorylation plays a key role in cellular signal transmission, metabolic regulation, cell cycle and other biological processes. In recent years, phosphorylation mass spectrometry has been widely used as an important tool for studying phosphorylation.

    • • Chemical Proteomics and Protein Expression Regulation

      To delve deeper into the diversity and functionality of proteins, the advent of chemical proteomics came about. Chemical proteomics uses chemical methods and mass spectrometry to decrypt the chemical composition, modifications, and regulatory expression of proteins at the molecular level.

    • • Exploring Protein Amino Acid Sequence Analysis: From Sequence to Function

      Protein amino acid sequence analysis is a key field in bioinformatics and molecular biology. By understanding the sequence of a protein, we can predict its three-dimensional structure, function, and interactions with other molecules. Below, we will delve into the process of protein amino acid sequence analysis: from sequence to function.

    • • The Advantages of Top-Down Proteomics in Quantitative Analysis

      Top-down proteomics is a novel approach to protein research, significantly different from the traditional bottom-up proteomics. Bottom-up proteomics first decomposes proteins into peptides, then performs mass spectrometric analysis on these peptides, and finally integrates this information to infer the structure and function of proteins. In contrast, top-down proteomics directly performs mass spectrometric analysis on the entire protein, thereby obtaining comprehensive information about the protein.

    • • Mass Spectrometry of Peptides and Its Applications in Biochemistry and Proteomics

      Mass spectrometry analysis is an analytical technique that determines the composition and structure of compounds by measuring the mass of molecular ions. In biochemistry and proteomics, mass spectrometry has become one of the main methods for analyzing peptides and proteins.

    • • Exploring Antibody Sequencing Tech: Insights into Immune Response

      Antibody sequencing involves the analysis of the amino acid sequence of an antibody, including the variable (V) and constant (C) regions. The variable region is often the focus of study as it contains the complementarity-determining regions (CDRs) responsible for the antibody's specificity in binding to antigens. This information helps us gain a deeper understanding of immune responses and how antibodies function by recognizing and binding to antigens specifically.

    • • Edman Degradation: Techniques for N-Terminal Amino Acid Sequencing of Proteins and Peptides

      Edman degradation is a method used to determine the N-terminal amino acid sequence of small peptides and proteins. This method is based on the periodic removal of amino acids from the N-terminus of the peptide chain and the identification of the removed amino acid. This process can be repeated to continuously determine the sequence of multiple amino acids.

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