Protein Oxidative Modification Analysis Service

    Protein oxidative modifications are generally induced by reactive oxygen species (ROS) such as superoxide anions, hydrogen peroxide, and hydroxyl radicals. These ROS are generated through multiple pathways in living organisms, including mitochondrial respiration, enzymatic redox reactions, and exposure to radiation. While protein oxidative modification is a natural physiological process, excessive ROS production or insufficient removal can cause excessive oxidation, impairing protein function and potentially leading to cellular damage.


    Advancements in molecular biology and biochemistry have positioned proteomics mass spectrometry as the primary method for investigating protein oxidative modifications. This technique allows for the precise identification of oxidatively modified amino acid residues and their chemical structures, facilitating detailed exploration into the types and mechanisms of these modifications. Employing mass spectrometry enables high-throughput screening and quantitative analysis of protein modification sites, offering crucial insights into cellular oxidative stress responses and the mechanisms underlying associated diseases.



    Lin, Y. S. et al. Anal. Chem. 2019.

    Figure 1. Proteomic Oxidative Modification Mass Spectrometric Analysis


    MtoZ Biolabs utilizes the Thermo’s Obitrap Fusion Lumos mass spectrometer in conjunction with Nano-LC technology to perform highly accurate analysis of protein oxidative modifications. This approach supports both quantitative and qualitative assessments, providing detailed information on modification types and locations. We accept a variety of protein samples and provide tailored one-stop solutions to meet diverse research needs. Free project evaluation!



    In the technical report, MtoZ Biolabs will provide you with detailed technical information, including:

    1. Experimental Procedures

    2. Relevant Experimental Parameters

    3. Detailed Information on Protein Oxidative Modifications

    4. Mass Spectrometry Images

    5. Raw Data

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