Cat: IPD-X40928

Recombinant Escherichia coli rpmH Protein ,GST

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Analytical Data

  • Gene name

    rpmH

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    rpmH; rimA; ssaF; b3703; JW3680; 50S ribosomal protein L34; Large ribosomal subunit protein bL34

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0A7P5

  • Expression Region

    1-46aa

  • Molecular Weight

    32.4 kDa

  • 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

Recombinant proteins have become essential tools in biotechnology, medicine, and research due to their specific functions and potential therapeutic applications. Among these proteins, rpmH, a component of the ribonucleoprotein complex involved in ribosome assembly, has garnered significant interest. The study of rpmH is particularly relevant because it plays a critical role in the biogenesis of ribosomes, which are vital for protein synthesis in all living organisms. Understanding the structure and function of rpmH can provide insights into the mechanisms of ribosomal assembly and function, with implications for understanding diseases associated with ribosomal dysfunction. Moreover, the ability to produce rpmH as a recombinant protein enables researchers to investigate its biochemical properties, interactions, and potential as a target for drug development. As such, the exploration of rpmH in recombinant form not only enhances our understanding of fundamental biological processes but also contributes to the advancement of therapeutic strategies against disorders linked to ribosomal anomalies.

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