Cat: IPD-X41721

Recombinant Mycobacterium tuberculosis rplB Protein ,His

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Analytical Data

  • Gene name

    rplB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Mycobacterium tuberculosis

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P9WHA5

  • Expression Region

    1-280aa

  • Molecular Weight

    34.7 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

RplB, a crucial component of the ribosomal protein family, plays a vital role in the assembly of the ribosome, the molecular machine responsible for protein synthesis in cells. The rplB gene encodes the L2 ribosomal protein, which is integral to ensuring proper ribosome structure and function. Understanding the role of RplB in ribosome biogenesis and its interactions with RNA and other ribosomal proteins is essential, as any dysfunction in ribosomal components can lead to ribosomopathies and various diseases, including cancer. Recent studies have focused on the recombinant expression of RplB in heterologous systems, allowing for detailed biophysical and structural analyses. These investigations help elucidate the protein’s role in ribosome assembly and its contribution to translational fidelity and efficiency. Furthermore, insights gained from RplB studies may aid in the development of new antibiotics targeting ribosomal functions, offering potential therapeutic strategies against bacterial infections. Overall, research on RplB recombinant protein fosters a deeper understanding of ribosomal dynamics and the molecular mechanisms underlying protein synthesis, making it a critical area of interest in molecular biology and biochemistry.

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