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    Phosphoproteomics Service

      Phosphoproteomics primarily encompasses quantitative phosphoproteomics analysis and phosphosite analysis. Utilizing advanced mass spectrometry technologies, quantitative phosphoproteomics accurately measures changes in protein phosphorylation levels, uncovering the dynamic regulatory mechanisms of cellular signal transduction. Meanwhile, phosphosite analysis identifies specific phosphorylation sites, elucidating the molecular basis of protein function regulation. These analyses contribute to a comprehensive mapping of phosphorylation networks, the identification of key regulatory events, and a deeper understanding of cellular biological processes and their aberrant manifestations in diseases. Phosphoproteomics provides high-resolution information on protein modifications, promotes the discovery of biomarkers and drug targets, accelerates the development of disease diagnostics and therapeutic strategies, and enhances research efficiency and data reliability through its high-throughput and high-sensitivity characteristics. 

       

      Service at MtoZ Biolabs

      MtoZ Biolabs offers phosphoproteomics service made up of two core aspects: quantitative phosphoproteomics analysis and phosphosite analysis. MtoZ Biolabs' high-throughput and high-sensitivity analysis methods can efficiently screen and validate key phosphorylation events in large-scale samples, significantly enhancing research efficiency and data reliability. With its advanced technical platform and professional service team, MtoZ Biolabs possesses diverse analytical platforms and extensive experience in phosphoproteomics. If you are interested in our services, please feel free to contact us.

       

      Service Advantages

      1. State-of-the-Art Mass Spectrometry Technology  

      MtoZ Biolabs' phosphoproteomics services employs the latest high-resolution mass spectrometers (such as LC-MS/MS), significantly enhancing the detection sensitivity of phosphorylation sites. This enables precise analysis in scenarios with limited sample amounts or low-abundance model systems.

       

      2. Efficient Phosphorylation Site Enrichment and Quantitation 

      Targeting key phosphorylation sites, MtoZ Biolabs utilizes high-affinity enrichment reagents and quantitative mass spectrometry methods to accurately identify and quantify low-abundance phosphorylation sites. This approach facilitates the elucidation of complex signaling networks.

       

      3. One-Time-Charge

      Our pricing is transparent, no hidden fees or additional costs.

       

      4. High-Data-Quality

      Deep data coverage with strict data quality control. AI-powered bioinformatics platform integrates all phosphoproteomics data, providing clients with a comprehensive data report.

       

      Case Study

      1. Quantitative Phosphoproteomic Profiling of Mouse Sperm Maturation in Epididymis Revealed Kinases Important for Sperm Motility

      Researchers analyzed the dynamic changes and regional specificity of protein phosphorylation during epididymal maturation of mouse sperm. As sperm mature from the caput to the cauda, there is a significant increase in protein tyrosine phosphorylation levels (Figure B). This change is further validated by correlation analysis of protein expression and phosphorylation levels (Figure D) and principal component analysis (Figure E), revealing distinct phosphorylation states in different epididymal regions. Additionally, comparison of phosphorylation sites with databases (Figure C) identified a large number of novel phosphorylation sites, providing new insights into the mechanisms of sperm maturation. These results demonstrate that sperm from different epididymal regions exhibit closely related and dynamic changes in morphology, phosphorylation states, and protein expression, highlighting the critical role of phosphorylation in the sperm maturation process.

       

      MtoZ Biolabs-Phosphoproteomics Service1

      Zhang, X. et al. Mol Cell Proteomics. 2024.

       

      2. Phosphoproteomic Analysis Reveals CDK5-Mediated Phosphorylation of MTDH Inhibits Protein Synthesis in Microglia

      A study using the Cdk5 knockout model successfully identified a large number of phosphorylation sites and, through rigorous quantitative analysis, revealed significant changes in upregulated and downregulated sites, highlighting the critical role of Cdk5 in regulating protein phosphorylation. This demonstrates that phosphoproteomics provides powerful support for understanding the dynamic regulatory mechanisms of cellular signaling pathways and the functions of specific proteins, while also exhibiting the advantages of large-scale data, high precision, and profound biological significance.

       

      MtoZ Biolabs-Phosphoproteomics Service2

      Shen, J. et al. Biochem Biophys Res Commun. 2024.

       

      Applications

      1. Disease Research: In cancer, autoimmune diseases, and neurodegenerative disorders, analyzing protein phosphorylation patterns reveals abnormalities in disease-related signal transduction and molecular mechanisms, helping to identify potential biomarkers and therapeutic targets.

       

      2. Drug Development: Phosphoproteomics can be used to assess the impact of drugs on cellular signaling pathways, optimize drug design, enhance drug efficacy, and reduce side effects.

       

      3. Integration of Basic Research and Clinical Applications: This analysis can provide high-resolution information on protein modifications, facilitating the translation of basic research findings into clinical applications.

       

      FAQ

      1. How does the instability of the phosphate group during collision-induced dissociation affect the accurate identification and localization of phosphorylation sites?

      Specific mass spectrometry techniques such as higher-energy collision-induced dissociation (HCD) or electron-transfer higher-energy collision-induced dissociation (EThcD) can be employed to enhance the retention and recognition efficiency of phosphorylation sites. Additionally, combining multiple fragmentation methods and utilizing specialized software algorithms can more accurately resolve phosphorylation sites, reducing identification errors caused by the loss of phosphate groups, thereby ensuring the accurate localization of phosphorylation sites.

       

      Deliverables

      1. Comprehensive Experimental Details

      2. Materials, Instruments, and Methods

      3. Relevant Liquid Chromatography and Mass Spectrometry Parameters

      4. The Detailed Information of Phosphoproteomics

      5. Mass Spectrometry Image

      6. Raw Data

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