Cat: IPD-X40969

Recombinant Human RPA4 Protein ,His

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Analytical Data

  • Gene name

    RPA4

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Replication factor A protein 4 ;RF-A protein 4

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q13156

  • Expression Region

    1-260aa

  • Molecular Weight

    32.8 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

RPA4, or replication protein A4, is a crucial component of the eukaryotic DNA replication machinery, playing a significant role in maintaining genomic stability during DNA replication and repair processes. RPA, a heterotrimeric protein complex, is essential for single-stranded DNA binding, eventually influencing various biological processes, including DNA repair, replication, and recombination. The RPA4 subunit has garnered research interest due to its unique structural properties, which may contribute to the overall functionality of the RPA complex. Dysregulation or mutations in RPA components, including RPA4, have been associated with several diseases, particularly cancer, highlighting its relevance in oncological research. Studying recombinant RPA4 proteins is vital for understanding its interactions with other protein partners involved in DNA processes, as well as for exploring its potential as a therapeutic target. Researchers have focused on expressing and purifying RPA4 to investigate its biochemical properties, binding mechanisms, and structural characteristics, in order to elucidate its role in the larger context of DNA metabolism. Furthermore, insights gained from RPA4 studies may unlock new strategies for cancer treatment, as targeting DNA repair pathways could lead to enhanced therapeutic efficacy.

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