Cat: IPD-X39460

Recombinant Human RALA Protein,His

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Analytical Data

  • Gene name

    RALA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    RAL; RAS-Like Protein A; Ras-Related Protein Ral-A; Ras Family Small GTP Binding Protein RALA

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P11233

  • Expression Region

    Met1~Leu206

  • Molecular Weight

    27kDa

  • 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

RALA, a member of the RAS superfamily of small GTPases, plays a crucial role in various cellular processes, including cell proliferation, differentiation, and migration. Its function is particularly significant in the context of cancer, where dysregulation of RALA activity can contribute to tumorigenesis and metastasis. Research into RALA has gained momentum due to its potential as a therapeutic target and as a biomarker for certain cancer types. The study of RALA’s structure and function through recombinant protein techniques has provided insights into its molecular mechanisms. By expressing and purifying RALA as a recombinant protein, researchers aim to investigate its interactions with downstream effectors and regulators, elucidating its role within intracellular signaling pathways. This can help identify novel intervention points for cancer treatment and enhance understanding of RALA's contributions to cell biology. Moreover, the development of RALA-specific inhibitors could pave the way for innovative therapeutic strategies. Overall, RALA recombinant protein research not only offers a deeper understanding of its physiological roles but also opens avenues for targeted therapies in oncological contexts.

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