Cat: PA1000-1344

Recombinant Human GST Protein,His

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Analytical Data

  • Gene name

    GST

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MGST2;GST2;Microsomal glutathione S-transferase 2

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O43916

  • Expression Region

    168-267aa

  • AA Sequence

    PPGPADLVLEEGDCVRKCGLLNLTVAAEACRERSHVAIKTVRVPEVNDLR ALVEDPRLNLKVIQLVRDPRGILASRSETFRDTYRLWRLWYGTGRKPYNL

  • Molecular Weight

    37 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

Glutathione S-transferases (GSTs) are a family of enzymes that play a crucial role in cellular detoxification by catalyzing the conjugation of glutathione to a variety of xenobiotics and endogenous compounds. They are essential for protecting cells from oxidative stress and are involved in various metabolic pathways. Research on GSTs has expanded due to their significance in pharmacology, toxicology, and cancer biology, as alterations in GST expression can influence drug metabolism and susceptibility to toxins. Additionally, certain GST isoforms have been implicated in the development of multidrug resistance in cancer cells, making them potential targets for therapeutic intervention. The study of GST proteins, especially through methods such as recombinant protein expression and purification, allows scientists to investigate their structure-function relationships, enzymatic mechanisms, and potential as biomarkers or drug targets. Recent trends in GST research also focus on their roles in signaling pathways, the interaction with other proteins, and their involvement in various diseases, including inflammation and neurodegeneration. This growing body of knowledge highlights the importance of GSTs in both basic and applied biomedical research, underscoring the need for continued investigation into their biochemical properties and therapeutic applications.

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