Cat: IPD-X39021

Recombinant Human CPZ Protein,His

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Analytical Data

  • Gene name

    CPZ

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q66K79

  • Expression Region

    Met425~Tyr652

  • Molecular Weight

    29KDa

  • 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

CPZ (Cobalt-Promoted Zinc) recombinant proteins have garnered significant attention in recent years due to their unique structural and functional properties, which make them valuable in various biotechnological and biomedical applications. These proteins, which derive from the combination of cobalt and zinc, exhibit enhanced catalytic activities and stability under extreme conditions compared to their wild-type counterparts. Research into CPZ proteins has been propelled by their potential applications in enzyme engineering, drug design, and therapeutic interventions. The ability to modulate their properties through genetic engineering opens new avenues for the development of tailored enzymes that can be used in industrial processes or as targeted drug delivery systems. Recent advances in recombinant DNA technology have further facilitated the production of CPZ proteins, enabling researchers to explore their functionalities in detail. As the demand for innovative biomolecules grows, understanding the complex interactions and mechanisms underlying CPZ protein behavior remains a key area of research, with implications for improving health outcomes and industrial efficiencies.

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