Cat: IPD-X40323

Recombinant Escherichia coli nikR Protein ,His

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Analytical Data

  • Gene name

    nikR

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    nikR; yhhG; b3481; JW3446Nickel-responsive regulator

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0A6Z6

  • Expression Region

    1-133aa

  • Molecular Weight

    19.1 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

NikR is a crucial metalloregulator that plays a significant role in the homeostasis and transport of nickel ions in various prokaryotic organisms. Nickel is an essential trace element required for the activity of certain metalloenzymes, but in excess, it can be toxic. The regulation of nickel levels is vital for microbial survival and adaptation, which is where NikR comes into play. This protein functions by binding nickel ions, altering its conformation, and interacting with DNA to modulate the expression of genes involved in nickel uptake and efflux. Research on the recombinant form of NikR has gained attention due to its potential applications in biotechnology and environmental science, particularly in bioremediation efforts to detoxify nickel-contaminated environments. Additionally, understanding the mechanism of NikR's regulation and its signaling pathways can provide insights into broader aspects of metal ion homeostasis and microbial physiology. The study of NikR, therefore, not only sheds light on microbial metal resistance mechanisms but also holds promise for developing novel strategies to tackle metal pollution and enhance metal recovery processes in biotechnological applications.

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