Cat: IPD-X33590

Recombinant Human Glutathione synthetase/GSS Protein,His

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Analytical Data

  • Gene name

    Glutathione synthetase/GSS

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Glutathione synthase

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P48637

  • Expression Region

    Asp268~Val474

  • Molecular Weight

    27/24kDa

  • 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

Glutathione synthetase (GSS) is a crucial enzyme in the biosynthesis of glutathione, a vital tripeptide that plays a significant role in cellular antioxidant defense and detoxification processes. Glutathione is essential for maintaining redox balance, protecting cells from oxidative stress, and supporting various metabolic functions. Deficiencies in GSS can lead to impaired glutathione synthesis, resulting in heightened susceptibility to oxidative damage and various diseases, including neurodegenerative disorders and cancer. Thus, the study of recombinant GSS protein is critical for understanding its structure and function, as well as its regulatory mechanisms in relevant biological contexts. By producing and characterizing recombinant GSS, researchers aim to elucidate the enzyme’s catalytic mechanism, identify potential inhibitors, and explore its activity in pathological conditions. Furthermore, recombinant GSS can serve as a valuable tool for therapeutic applications, such as developing drugs that enhance glutathione levels in diseases associated with oxidative stress. Overall, the research on GSS not only deepens our understanding of cellular defense mechanisms but also opens avenues for novel therapeutic strategies aimed at combating oxidative-stress-related diseases.

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