Cat: IPD-X40532

Recombinant Mouse Septin9 Protein ,His

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Analytical Data

  • Gene name

    Septin9

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    SL3-3 integration site 1 protein Kiaa0991, Sint1

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q80UG5

  • Expression Region

    1-583aa

  • Molecular Weight

    69.6 kDa

  • 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.

Quality inspection process

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Protein Description

Septin9 is a member of the septin family of GTP-binding proteins, which play a crucial role in various cellular processes, including cytokinesis, cell division, and cytoskeletal organization. Recent studies have highlighted its potential as a biomarker for early detection of colorectal cancer, as altered expression levels of Septin9 have been associated with tumorigenesis. The recombinant form of Septin9 has become an important research tool, enabling scientists to investigate its biochemical properties, structural characteristics, and interactions with other cellular proteins. By producing Septin9 as a recombinant protein, researchers can better understand its function in normal physiology and disease states, as well as evaluate its utility in diagnostic applications. Additionally, studies utilizing recombinant Septin9 may provide insights into its role in cellular signaling pathways, offering potential therapeutic targets for cancer treatment. The development of assays and biochemical methods to study recombinant Septin9 is crucial for advancing our understanding of this protein's involvement in cancer progression and for exploring its potential use in clinical settings. Overall, the ongoing research on Septin9 recombinant protein not only enhances our comprehension of its biological significance but also opens new avenues for cancer research and diagnostic innovation.

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