Kinase Interactome Platform

Kinase Interactome Platform

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Kinase Interactome Platform


Protein-protein interactions (PPIs) play a central role in all cellular processes. As an important component of PPIs, kinases are key regulators of diverse fundamental cellular processes. Therefore, studying the interactions of kinases with different substrates, proteins, and other molecules to increase the understanding of cellular signaling mechanisms is essential for biological research as well as for many areas of biological and medical research. Dissecting the comprehensive kinase interactome to establish dynamic interaction networks under appropriate cellular conditions will provide the basis for further understanding of the different biological roles of kinases.

Creative BioMart combines in silico, in vitro, and in vivo strategies for protein interaction analysis with bioinformatics approaches to provide our customers with a global view of kinase interaction networks. Our team of scientists with extensive experience in kinase interaction analysis and cell signaling research is dedicated to helping our customers identify critical nodes in kinase interaction networks to advance their research to the next stage.

Exploring Our Kinase Interactome Platform

  • Virtual Interactomics

    Computational tools allow for the in silico prediction, simulation, and networking of kinase interactions for extensive assembly of large-scale protein-protein interactions and subgraphs with dynamical properties.

  • Quantitative Interactomics

    Provide valuable insights into the precise kinase regulatory networks by accurately measuring protein abundance, quantifying specific interactions, and determining the stoichiometry of these interactions.

  • Functional Interactomics

    Combine proteomics, bioinformatics, and systems biology to identify kinase interaction networks and annotate protein functions to achieve a better understanding of biological systems.

  • Comparative Interactomics

    Provide opportunities to compare kinase interaction networks under different conditions due to genetic or environmental changes or between different tissues, organelles, and species.

Applications of Our Kinase Interactome Platform

  • Biological Research

    Uncovering kinase interactions involved in numerous cellular functions and pathological processes is necessary for understanding complex biological systems.

  • Disease Research

    Uncovering dynamic changes of kinase interactions related to diseases have obvious implications for unraveling the pathogenesis of diseases and developing novel treatments.

  • Biomarker Discovery

    Analyzing disease-related kinase interactomes and involved differentially expressed genes or proteins to provide a functional context for discovering potential biomarkers.

  • Drug Discovery

    Applying interactomics to discover disease-relevant kinase interactions and pathogen-host interactions can facilitate drug target discovery and obtain optimized lead compounds with improved selectivity and specificity.

Benefits of Our Phosphoproteomics Platform

  • Highly Integration

    Highly Integration

    Integrating a wide range of assays/techniques, bioinformatics strategies, and interactome databases for comprehensive profiling in vitro and in vivo kinase interactomes.

  • Wide Applicability


    A high-throughput platform for measuring spatiotemporal changes in the kinase interactome with the advantages of high sensitivity, high speed, and low cost.

  • High Flexibility

    Broad Applications

    Interactome analysis can be performed on almost all kinds of kinases from different species to achieve different purposes in biological and biomedical research.

  • Professional Data Analysis

    Professional Data Analysis

    An experienced scientific team is dedicated to uncovering key information from the vast amount of interactomics data and experimental results.

Take the Next Step

See how our advanced technology platform can help you maintain your leading position in kinase research and drug development.