Cat: IPD-X40692

Recombinant Human HPF1 Protein ,His & SUMO

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Analytical Data

  • Gene name

    HPF1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    C4orf27

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9NWY4

  • Expression Region

    1-346aa

  • Molecular Weight

    59.4 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

HPF1, or Histone Paralogous Factor 1, has emerged as a significant player in the field of chromatin biology and epigenetic regulation. This protein is critically involved in the modulation of histone modifications, particularly in the context of DNA repair and transcriptional regulation. Recent studies have illuminated its role in enhancing the activity of histone-modifying enzymes, thereby influencing chromatin accessibility and the assembly of various protein complexes at DNA regulatory elements. The understanding of HPF1's function is rapidly evolving as researchers uncover its interactions with key histone marks, such as histone H3 lysine 36 methylation, which is crucial for orchestrating the response to DNA damage. Investigating HPF1's mechanism of action not only provides insight into fundamental cellular processes but also holds potential implications for understanding diseases linked to epigenetic dysregulation, including cancer. Given its importance in maintaining genome integrity and regulating gene expression through chromatin dynamics, HPF1 is positioned as a promising target for therapeutic intervention and further research into its reconstituted protein forms has become a focal point in the pursuit of novel epigenetic modulators. This trajectory underscores the necessity of comprehensively exploring HPF1's structural and functional characteristics to fully elucidate its biological roles and therapeutic potential.

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