Cat: PA2000-2640

Recombinant E.coli dps Protein,His

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Analytical Data

  • Gene name

    dps

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    dps;DPS1;TPRT;All trans-polyprenyl-diphosphate synthase PDSS1

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0C558

  • Expression Region

    1-183aa

  • AA Sequence

    MTSFTIPGLSDKKASDVADLLQKQLSTYNDLHLTLKHVHWNVVGPNFIGVHEMIDPQVELVRGYADEVAERIATLGKSPKGTPGAIIKDRTWDDYSVERDTVQAHLAALDLVYNGVIEDTRKSIEKLEDLDLVSQDLLIAHAGELEKFQWFVRAHLESAGGQLTHEGQSTEKGAADKARRKSA

  • Molecular Weight

    36.3 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

DPS (dps stands for "DNA-binding protein from starved cells") is a unique protein that plays a crucial role in protecting bacterial cells from oxidative stress and DNA damage, particularly during periods of starvation or environmental stress. The study of DPS has gained attention due to its significant function in safeguarding cellular integrity under fluctuating conditions, which is vital for bacterial survival and adaptation. Researchers have found that DPS possesses the ability to bind to DNA and form ferritin-like complexes, thereby sequestering free iron and preventing the formation of harmful reactive oxygen species (ROS). Investigating the structural and functional aspects of DPS not only enhances our understanding of bacterial resistance mechanisms but also has broader implications in biotechnology and medicine, where the principles of oxidative stress response can be applied. Moreover, understanding DPS functionality could provoke novel approaches in developing antimicrobial agents or biotechnological applications, such as improving the stress tolerance of crops. As research continues to evolve, the potential of DPS as a target for therapeutics and its applications in synthetic biology are becoming increasingly significant.

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