Cat: IPD-X39201

Recombinant Human ARAF Protein,His

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Analytical Data

  • Gene name

    ARAF

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    A-RAF; ARAF1; PKS2; PKS; Serine/threonine-protein kinase A-Raf

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P10398

  • Expression Region

    Gln349~Pro606

  • Molecular Weight

    30kDa

  • 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

ARAF (Atypical Rho GTPase Activating Protein) is a member of the Rho family of GTPases, which play crucial roles in various cellular processes, including cytoskeletal dynamics, cell migration, and signal transduction. The study of ARAF has gained importance due to its potential implications in cancer biology, where abnormal ARAF activity can influence tumor progression and metastasis. Recent research has pointed towards the significance of ARAF in modulating pathways altered in various malignancies, making it a potential therapeutic target. Additionally, understanding the mechanistic role of ARAF in these pathways could provide insights into novel cancer treatments. The reconstitution of ARAF protein in vitro has become a focal point for researchers, allowing for the investigation of its interactions and function in cellular environments. By utilizing advanced techniques, such as CRISPR-Cas9 for gene editing and various biochemical assays, scientists aim to delineate the structure-function relationship of ARAF and its regulatory mechanisms. This research not only enhances our understanding of Rho GTPases but also paves the way for targeted therapies that could mitigate the detrimental effects of its dysregulation in disease contexts. Moreover, the exploration of ARAF's role in other physiological processes expands the horizon for its therapeutic potential beyond oncology, making it a critical subject of ongoing biological and medical research. Such investigations contribute to the broader understanding of GTPase signaling networks and their implications in health and disease, thereby highlighting the relevance of ARAF in both basic and applied sciences.

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