Cat: IPD-X39303

Recombinant Human MAST2 Protein,His & GST

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Analytical Data

  • Gene name

    MAST2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MAST205; MTSSK

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q6P0Q8

  • Expression Region

    Phe512~Phe785

  • Molecular Weight

    61kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

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Protein Description

MAST2 (microtubule-associated serine/threonine kinase 2) is a member of the MAST (Microtubule Associated Serine/Threonine Kinase) family, which plays a crucial role in cellular processes such as microtubule organization, cell signaling, and neuronal function. Research into MAST2 is driven by its involvement in various physiological and pathological processes, including its potential link to neurodevelopmental disorders and cancer. It is characterized by its unique structure, featuring a kinase domain that enables it to phosphorylate specific substrates, thereby modulating their activity and localization within the cell. Studies have demonstrated that MAST2 is expressed in multiple tissues, with particularly high levels in the brain, underscoring its importance in neurobiological functions. Investigations into the regulatory mechanisms of MAST2, including its interaction with other cellular components and signaling pathways, are pivotal for understanding its role in health and disease. The generation of recombinant MAST2 proteins has been a key methodological approach, allowing researchers to perform biochemical assays and structural analyses, ultimately contributing to a more comprehensive understanding of its function. This research not only elucidates the fundamental biology of MAST2 but also holds potential for identifying novel therapeutic targets in related diseases, highlighting the significance of MAST2 in both basic research and clinical applications.

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