Cat: IPD-X40938

Recombinant Human GLO2 Protein ,GST

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Analytical Data

  • Gene name

    GLO2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Glyoxalase II ;Glx II

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q16775

  • Expression Region

    50-308aa

  • Molecular Weight

    55.7 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

GLO2, or glyoxalase 2, is an enzyme that plays a crucial role in the detoxification of reactive aldehydes, specifically methylglyoxal, which is a byproduct of glycolysis and is known to cause cellular damage. The significance of GLO2 in various biological processes, including cellular response to oxidative stress and its implications in diseases such as diabetes, neurodegeneration, and cancer, has garnered increasing research interest. In recent years, studies have highlighted the potential of GLO2 as a therapeutic target, emphasizing the need for a deeper understanding of its structure and function. The recombinant expression of GLO2 allows for the study of its enzymatic activity, interactions, and potential inhibitors, providing insights into its role in cellular metabolism and pathophysiology. Moreover, the ability to produce large quantities of GLO2 through recombinant techniques facilitates high-throughput screening of compounds that could modulate its activity, thus opening avenues for drug development. By elucidating the mechanism of action of GLO2 and its involvement in disease processes, researchers aim to identify novel strategies for therapeutic intervention, making it a promising candidate for further investigation in the context of metabolic disorders and cancer therapy.

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