Cat: IPD-X41159

Recombinant Chlorobaculum tepidum ppk2 Protein ,His & Myc

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Analytical Data

  • Gene name

    ppk2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ATP-polyphosphate phosphotransferase 2 Polyphosphoric acid kinase 2

  • Species

    Chlorobaculum tepidum

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O68984

  • Expression Region

    140-343aa

  • Molecular Weight

    34.4 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

PPK2, or polyphosphate kinase 2, is a crucial enzyme in the regulation of polyphosphate metabolism within various organisms, including bacteria, archaea, and eukaryotes. It catalyzes the conversion of ATP and inorganic phosphate into polyphosphate chains, which serve several important cellular functions, including energy storage, cellular signaling, and stress response. Research on PPK2 has gained prominence due to its significant roles in microbial physiology and its potential applications in biotechnology and medicine. For instance, manipulation of polyphosphate levels through PPK2 could enhance microbial production processes, bioremediation efforts, and even industrial enzyme production. In addition, PPK2 has been linked to virulence in certain pathogens, making it a target for the development of novel antimicrobial agents. Understanding the structure, function, and regulatory mechanisms of PPK2 is thus essential for both basic biological research and practical applications. As advances in recombinant protein technology allow for the effective production and analysis of PPK2, researchers are increasingly focused on characterizing this enzyme to reveal its functional properties and potential as a biotechnological tool. This research not only deepens our understanding of polyphosphate metabolism but also opens new avenues for innovative therapeutic strategies and industrial processes, highlighting the multifaceted significance of PPK2 in modern science.

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