Cat: IPD-X39966

Recombinant Human RAF1 Protein ,His & SUMO

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Analytical Data

  • Gene name

    RAF1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Proto-oncogene c-RAF ;cRafRaf-1

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P04049

  • Expression Region

    1-648aa

  • Molecular Weight

    89.1 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.

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Protein Description

RAF1, a key member of the RAF (Rapidly Accelerated Fibrosarcoma) family of serine/threonine kinases, plays a crucial role in the RAS-RAF-MEK-ERK signaling pathway, which is pivotal for regulating cell growth, differentiation, and survival. Aberrant activation of RAF1 is implicated in various cancers, making it a significant target for therapeutic intervention. Research has increasingly focused on the recombinant expression of RAF1 proteins to elucidate their structure-function relationships and mechanisms of action. Recombinant RAF1 proteins are instrumental in both in vitro and in vivo studies, allowing researchers to investigate the effects of specific mutations, post-translational modifications, and interactions with signaling partners. By employing techniques such as site-directed mutagenesis, researchers are able to generate RAF1 variants that help to map the functional domains critical for its kinase activity and downstream signaling. Moreover, the development of RAF1 inhibitors has become a major area of interest in cancer therapeutics, highlighting the importance of understanding RAF1 biology at a molecular level. This groundwork lays the foundation for ongoing studies aimed at developing targeted therapies that can effectively inhibit aberrant RAF1 signaling pathways in cancer, offering potential for improved treatment strategies. Overall, the research on recombinant RAF1 proteins not only sheds light on its fundamental biological roles but also drives the quest for innovative therapeutic approaches in managing RAS-driven malignancies.

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