Cat: IPD-X38936

Recombinant Mouse NRIP2 Protein,His & GST

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Analytical Data

  • Gene name

    NRIP2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9JHR9

  • Expression Region

    Met1~Ala270

  • Molecular Weight

    60kDa

  • 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.

Quality inspection process

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Protein Description

NRIP2, or Nuclear Receptor Interacting Protein 2, is a vital co-regulator involved in various cellular processes, including transcription regulation, signal transduction, and cellular response to hormonal signals. It interacts with multiple nuclear receptors, influencing gene expression patterns that are crucial in metabolic processes, development, and disease states. Research has highlighted the role of NRIP2 in several pathological conditions, including obesity, diabetes, and cancer, where its regulatory function on nuclear receptors may enhance or inhibit oncogenic pathways. Furthermore, NRIP2's potential as a therapeutic target has garnered attention, prompting studies on its structural and functional properties through recombinant protein expression. The use of recombinant NRIP2 allows for detailed investigations into its biochemical interactions and structural characteristics, facilitating the development of targeted therapies. Understanding the role of NRIP2 at the molecular level may provide insights into novel strategies for modulating nuclear receptor activity, ultimately contributing to the advancement of innovative treatments for metabolic and neoplastic disorders. As such, the study of NRIP2 recombinant protein is not only significant for elucidating fundamental biological mechanisms but also holds promise for therapeutic innovations.

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