Cat: PA2000-2594

Recombinant E.coli h1f0-a Protein,His

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Analytical Data

  • Gene name

    h1f0-a

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    h1f0-a;

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P22845

  • Expression Region

    1-194aa

  • AA Sequence

    MTENSAPAAKPRRSKASKKSTDHPKYSDMILDAVQAEKSRSGSSRQSIQKYIKNNYTVGENADSQIKLSIKRLVTSGTLKQTKGVGASGSFRLAKADEVKKPAKKPKKEIKKAVSPKKAAKPKKAAKSPAKAKKPKVAEKKVKKAPKKKPAPSPRKAKKTKTVRAKPVWASKAKKAKPSKPKAKASPKKSGRKK

  • Molecular Weight

    37.0 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.

Quality inspection process

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Protein Description

The H1F0-A protein, a member of the histone family, plays a crucial role in the regulation of gene expression and chromatin structure. Research into H1F0-A has gained momentum due to its involvement in various cellular processes, including DNA compaction, transcriptional regulation, and responses to environmental stress. Notably, alterations in histone proteins, particularly H1 variants, have been implicated in numerous diseases, including cancer. Understanding the functional dynamics of H1F0-A is essential for elucidating its specific contributions to chromatin architecture and gene regulation. Additionally, studies have shown that H1F0-A may influence cellular differentiation and proliferation, highlighting its potential as a therapeutic target. Investigations often focus on the molecular mechanisms by which H1F0-A interacts with other proteins and nucleic acids, as well as its post-translational modifications, which can affect its stability and function. Furthermore, research is exploring the role of H1F0-A in the context of epigenetic modifications, providing insights into how these changes are linked to cellular identity and disease states. Overall, the research background of H1F0-A underscores its significance in epigenetics and gene regulation, paving the way for further exploration of its potential therapeutic applications.

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