Cat: IPD-X41129

Recombinant Mouse Gpx7 Protein ,His & Myc

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Analytical Data

  • Gene name

    Gpx7

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    /

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His & C- MYC

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q99LJ6

  • Expression Region

    19-186aa

  • Molecular Weight

    26.7 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

Gpx7, or Glutathione Peroxidase 7, is a member of the glutathione peroxidase family, which plays a crucial role in cellular oxidative stress response by catalyzing the reduction of hydrogen peroxide and organic peroxides. This enzyme is particularly interesting due to its potential involvement in various physiological processes, including cell migration, proliferation, and apoptosis. Recent studies have indicated that Gpx7 may be linked to the pathogenesis of several diseases, particularly cancer, as its expression levels can be altered in tumor tissues. Moreover, Gpx7 is believed to contribute to the regulation of the redox state of the cell, impacting not only antioxidant defense mechanisms but also signaling pathways related to cellular stress responses. Researchers are increasingly focused on recombinant Gpx7 protein to investigate its biochemical properties, enzyme kinetics, and structural characteristics, as well as to explore its therapeutic potential. By studying the recombinant form of this protein, scientists aim to elucidate its functionality and interactions within the cellular environment, paving the way for novel insights into its role in health and disease. The growing interest in Gpx7 is underscored by its potential application in developing antioxidant therapies and understanding the molecular underpinnings of oxidative stress-related conditions.

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