Protein Characterization Service

    Proteins serve as the carriers of life substances and executors of biological functions, playing a crucial role in maintaining normal physiological activities of organisms. Protein characterization analysis involves the characterization of protein purity, molecular weight, structure, post-translational modifications, and interactions, among others. As one of the core areas in biological science research, protein characterization analysis reveals how proteins function within biological systems and how they interact to maintain normal physiological functions.


    Common methods for protein characterization analysis include nuclear magnetic resonance (NMR), mass spectrometry (MS), and Western blotting (WB). NMR is commonly used to study the three-dimensional structure and dynamic properties of proteins. MS analyze the molecular weight, post-translational modifications, and interactions of proteins. While WB utilizes specific antibodies to detect distances and interactions between proteins.


    Services at MtoZ Biolabs

    1. Protein Purity Analysis

    Various purity analysis methods are available, including SDS-PAGE, capillary electrophoresis, zinc reverse staining, glutaraldehyde-modified silver staining, and MALDI-TOF-MS. These methods are utilized to detect contaminants, protein variants, isoforms, S-S bond mismatches, truncated proteins, degraded proteins, protein modifications, protein aggregates, and protein precursors.


    2. Protein Molecular Weight Analysis

    Protein complexes and protein-small molecule complex molecular weights are determined using techniques such as gel permeation chromatography, SDS-PAGE, and mass spectrometry.


    3. Protein Structure Identification

    Characterization of top-down protein primary structure (including amino acid composition analysis, peptide sequence analysis, and disulfide bond localization) is performed based on Thermo Fisher's Orbitrap Fusion Lumos mass spectrometry platform combined with nanoLC-MS/MS chromatography, as well as protein spatial configuration determination based on circular dichroism spectroscopy.


    4. Protein Post-Translational Modification Analysis

    Multiple mass spectrometry platforms (Thermo Fisher's Q Exactive HF, Orbitrap Fusion, and Orbitrap Fusion Lumos mass spectrometry platforms combined with Nano-LC) are employed for the identification of protein phosphorylation, glycosylation, ubiquitination, acetylation, methylation, disulfide bond formation, nitrosylation, and among other post-translational modifications.


    5. Protein Interaction Analysis and Identification of Interacting Proteins

    Techniques such as WB, immunoprecipitation (IP), and GST-pull-down are utilized to study protein-protein interactions. LC-MS/MS is employed for mass spectrometric identification analysis of proteins/protein complexes in IP, Co-IP samples, and GST fusion protein pull-down purified samples.



    In the technical report, MtoZ Biolabs provides detailed technical reports, including:

    1. Experimental Procedures

    2. Relevant Mass Spectrometry Parameters

    3. Detailed information on protein characterization analysis

    4. Mass Spectrometry Images

    5. Raw Data

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