Protein Benzoylation Analysis

    Protein benzoylation is a novel lysine acylation modification that uniquely involves the attachment of a benzoyl group. As the only known lysine modification with a benzene ring, benzoylation is distinct from traditional acetylation. The benzoyl group is significantly larger, approximately twice the size of an acetyl group, and exhibits nearly three times the hydrophobicity. Each benzoylation event increases the protein's molecular weight by 104.0268 Da. This modification has profound effects on protein structure and function, particularly on histones, where it can influence gene expression and chromatin structure more strongly than acetylation. Additionally, benzoylation can also play crucial regulatory roles in non-histone proteins. 

     

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    Figure 1. Lysine Benzoylation

     

    Leveraging state-of-the-art mass spectrometry and advanced proteomic analysis, MtoZ Biolabs offers highly sensitive Protein Benzoylation Analysis services to help researchers investigate this emerging modification and its diverse biological functions.

     

    Analysis Workflow

     

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    Services at MtoZ Biolabs

    1. Targeted Protein Benzoylation Analysis

    MtoZ Biolabs provides Targeted Protein Benzoylation Analysis for clients who need to examine benzoylation on specific, predefined proteins. This service focuses on a single target or a small group of proteins designated by the customer. Through targeted protein enrichment and high-resolution LC-MS/MS, we accurately identify and quantify benzoylation sites, offering precise insights into site-specific regulatory mechanisms and their biological significance.

     

    2. Benzoylation Proteomics

    Benzoylation Proteomics, in contrast, provides a global view of benzoylation modifications across the entire proteome. Using high-throughput LC-MS/MS combined with benzoylated peptide enrichment, this service enables comprehensive mapping and quantitative comparison of benzoylation events in complex biological samples. It is ideal for system-level studies aimed at revealing regulatory pathways, biomarker candidates, and the broader functional impact of benzoylation in health and disease.

     

    Why Choose MtoZ Biolabs?

    1. Advance Analysis Platform: MtoZ Biolabs established an advanced protein PTM analysis platform, guaranteeing reliable, fast, and highly accurate analysis service.

    2. One-Time-Charge: Our pricing is transparent, no hidden fees or additional costs.

    3. High-Data-Quality: Deep data coverage with strict data quality control. AI-powered bioinformatics platform integrate PTM proteomics analysis data providing clients with a comprehensive data report.

    4. Wide Applicability: Suitable for various biological samples, including blood, urine, and tissues.

    5. Customized Solutions: We offer tailored services, from modification site identification to in-depth functional annotation, providing customized support to meet specific research objectives.

     

    Sample Submission Requirements

     

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    For more sample details, please consult our technical team.

    What Could be Included in the Report?

    1. Comprehensive Experimental Details

    2. Materials, Instruments, and Methods

    3. Total Ion Chromatogram & Quality Control Assessment (project-dependent)

    4. Data Analysis, Preprocessing, and Estimation (project-dependent)

    5. Bioinformatics Analysis

    6. Raw Data Files

     

    At MtoZ Biolabs, we are committed to delivering high-quality, high-throughput Protein Benzoylation Analysis services to help researchers unravel the complex regulatory mechanisms of post-translational modifications. Our expertise in proteomics and metabolomics positions us at the forefront of scientific discovery. For more information or inquiries, please contact us.

    MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.

    Related Services

    Post-Translational Modifications Proteomics Service

    Acylation Quantitative Proteomics Services

    Acylation Analysis Service

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