Cat: IPD-X30330

Recombinant Human HRAS Protein,His

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Analytical Data

  • Gene name

    HRAS

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HRAS1; K-Ras; N-Ras; RASH1; C-Bas/Has; H-Ras; Transforming protein p21

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P01112

  • Expression Region

    Phe82~Glu176

  • Molecular Weight

    15kDa

  • 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

HRAS (Harvey Rat Sarcoma Viral Oncogene Homolog) is a member of the RAS gene family, which plays a crucial role in cell signaling pathways that regulate cell growth, differentiation, and survival. Mutations in HRAS are commonly associated with various cancers, including bladder cancer, thyroid cancer, and head and neck cancers. Understanding the structure and function of HRAS is essential for developing targeted therapies, as its aberrant activity is linked to tumorigenesis. The study of HRAS recombinant proteins has gained attention in the field of molecular biology, as these proteins enable researchers to investigate the mechanistic insights into HRAS signaling and its interactions with downstream effectors. By producing recombinant HRAS proteins in various expression systems, scientists can perform biochemical assays, structural studies, and drug screening experiments. This research not only enhances our understanding of HRAS-related cancer pathways but also facilitates the identification of potential therapeutic targets. Additionally, the development of small molecules or peptide inhibitors that specifically target mutated HRAS holds promise for improving cancer treatment options. Overall, the study of HRAS recombinant proteins is a vital aspect of cancer research, aiming to elucidate the molecular underpinnings of oncogenesis and contribute to advancing targeted cancer therapies.

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