Cat: IPD-X25946

Recombinant Human PFDN5 Protein,GST

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Analytical Data

  • Gene name

    PFDN5

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    C-Myc-binding protein Mm-1Myc modulator 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q99471

  • Expression Region

    2-154aa

  • Molecular Weight

    44.2 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.

Quality inspection process

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Protein Description

PFDN5 (Prefoldin 5) is a member of the prefoldin family, which plays a crucial role in protein folding within cells. As a cytoplasmic chaperone, PFDN5 assists in the proper assembly of multi-subunit protein complexes by facilitating the correct folding of nascent polypeptides. Its importance is underscored by its involvement in key cellular processes, such as stress responses and cell proliferation. Recent studies have suggested that PFDN5 may have implications in various diseases, including cancer, where aberrant protein folding and accumulation of misfolded proteins can lead to tumorigenesis and poor patient prognosis. Additionally, PFDN5 has been linked to neurodegenerative disorders, highlighting its potential as a biomarker or therapeutic target. Understanding the structure and function of PFDN5, particularly through recombinant protein production, can provide insights into its role in health and disease, as well as its potential for biotechnical applications in protein engineering and drug development. Thus, research into PFDN5 not only expands our knowledge of cellular protein homeostasis but also opens up avenues for innovative treatments for diseases associated with protein misfolding.

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