Cat: IPD-X40858

Recombinant Human RPL15 Protein ,GST

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Analytical Data

  • Gene name

    RPL15

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    60S ribosomal protein L15; EC45; FLJ26304; ribosomal protein L15 ; RL15_HUMAN; RPL10; RPL15; RPLY10 ; RPYL10

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P61313

  • Expression Region

    2-204aa

  • Molecular Weight

    51 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

RPL15, a critical component of the ribosomal protein family, plays a fundamental role in ribosome biogenesis and protein synthesis. Its significance in cellular function has garnered attention due to its involvement in various biological processes, including cell growth and proliferation. Mutations or dysregulation of RPL15 have been linked to several diseases, particularly cancer, where altered ribosome function can contribute to tumorigenesis. Recent studies have focused on the expression and characterization of recombinant RPL15 protein to better understand its structural and functional properties. By producing this recombinant protein, researchers can investigate its interactions with other ribosomal proteins and RNA, elucidate its role in ribosome assembly, and explore potential implications in disease states. Additionally, RPL15 has been shown to possess a unique evolutionary conservation across species, indicating its critical function in ribosomal activity. Understanding RPL15 through recombinant protein studies provides valuable insights into fundamental biological mechanisms and may open avenues for therapeutic interventions targeting ribosomal dysfunctions. The study of RPL15 and its recombinant protein forms stands at the intersection of molecular biology and medicine, emphasizing its potential as both a biological marker and a target for novel therapeutic strategies.

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