Cat: IPD-X39292

Recombinant Rat NRN1 Protein,His

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Analytical Data

  • Gene name

    NRN1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Rat

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    -

  • Expression Region

    Ala28~Phe142

  • Molecular Weight

    16kDa

  • 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

N-Ras is a member of the Ras family of proteins, which are integral to cell signaling pathways that control cell growth, differentiation, and survival. Dysfunction or mutations in Ras proteins, particularly N-Ras, are implicated in various cancers, including melanoma, leukemia, and thyroid cancers. The study of recombinant N-Ras (NRN1) proteins has gained significant attention in recent years due to their potential as therapeutic targets and the need for better understanding of their structure-function relationships. Researchers are developing recombinant NRN1 proteins to investigate the biochemical mechanisms underlying Ras signaling, explore its role in tumorigenesis, and identify potential intervention strategies. Additionally, studying these recombinant proteins allows for the examination of the effects of specific mutations in Ras and the interaction with downstream effectors. Understanding these processes can lead to the development of novel drugs that can disrupt aberrant Ras signaling pathways. The advancement of techniques such as CRISPR/Cas9 and structural biology has also facilitated the exploration of NRN1, leading to more insights into its interactions and the identification of small molecules that can inhibit its activity. This research is crucial for developing targeted therapies that could improve outcomes for cancer patients with Ras-driven malignancies, ultimately contributing to the field of personalized medicine.

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