Cat: IPD-X40778

Recombinant Kluyveromyces marxianus RPB5 Protein ,His

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Analytical Data

  • Gene name

    RPB5

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    RPB5; DNA-directed RNA polymerases I; II; and III subunit RPABC1; RNA polymerases I; II; and III subunit ABC1

  • Species

    Kluyveromyces marxianus

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9P4B9

  • Expression Region

    1-215aa

  • Molecular Weight

    29.0 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

The RPB5 protein, a critical component of RNA polymerase II, plays a significant role in the transcription process of eukaryotic cells. Its essential function lies in maintaining the stability and activity of the RNA polymerase complex, which is responsible for synthesizing messenger RNA (mRNA) from DNA templates. Understanding RPB5 is pivotal for elucidating the mechanisms of gene expression regulation, which has implications in various biological processes and diseases. Recent research has focused on the recombinant expression of RPB5 to facilitate structural and functional studies, allowing scientists to investigate its interactions with other subunits of RNA polymerase and identify potential post-translational modifications. Additionally, the overexpression of RPB5 in heterologous systems provides valuable insights into its role in transcriptional regulation and the cellular response to stress. Given its involvement in critical pathways, RPB5 is also of interest in the context of cancer research, as alterations in transcriptional machinery can lead to abnormal gene expression patterns. Overall, the study of RPB5 not only enhances our understanding of the fundamental mechanisms of transcription but also opens up avenues for therapeutic interventions targeting transcriptional dysregulation in various diseases.

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