Cat: PA2000-2795

Recombinant Human hup1 Protein,His

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Analytical Data

  • Gene name

    hup1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    hup1;HUP1;Paired box Protein Pax-7

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0A3H6

  • Expression Region

    1-93aa

  • AA Sequence

    MNRSELVAALADRAEVTRKDADAVLAAFAEVVGDIVSKGDEKVTIPGFLTFERTHRAARTARNPQTGEPIQIPAGYSVKVSAGSKLKEAAKGK

  • Molecular Weight

    36.9 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

Hup1 protein, a significant member of the Hup family, has garnered attention in molecular biology and biotechnology due to its crucial role in diverse cellular processes and its potential applications in various fields. Initially identified in specific microorganisms, Hup1 plays an essential role in stress response and cellular regulation, acting as a chaperone that assists in protein folding and stability under adverse conditions. Recent studies have highlighted its involvement in the regulation of gene expression and its interactions with other proteins, suggesting a complex network of functional roles within the cell. Researchers are particularly interested in Hup1 due to its potential in bioremediation and its applications in the agricultural sector, where enhancing stress resistance in crops can lead to improved yields. Furthermore, understanding the structural and functional dynamics of Hup1 can pave the way for developing novel biotechnological tools, such as genetically modified organisms that can thrive in harsh environments. As research continues to unravel the intricacies of Hup1, its properties may offer exciting opportunities in synthetic biology, bioengineering, and therapeutic development. Overall, the Hup1 protein represents a promising subject for ongoing investigation, with significant implications for both fundamental science and practical applications.

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