Cat: IPD-X38302

Recombinant Human PPARg Protein,His

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Analytical Data

  • Gene name

    PPARg

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PPAR-G; PPARG1; PPARG2; NR1C3; Glitazone Receptor; Nuclear Receptor Subfamily 1 Group C Member 3

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P37231

  • Expression Region

    349~488aa

  • Molecular Weight

    16kDa

  • 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

PPARγ (Peroxisome Proliferator-Activated Receptor Gamma) is a crucial member of the nuclear receptor superfamily, playing a significant role in regulating glucose and lipid metabolism, as well as adipogenesis. Discovered in the late 1990s, PPARγ was initially identified as a key factor in fat cell differentiation. Its important role in metabolic diseases, particularly insulin resistance and type 2 diabetes, spurred extensive research. Activation of PPARγ by various ligands, including thiazolidinediones (TZDs), has shown promise in enhancing insulin sensitivity, making it a target for therapeutic intervention in metabolic disorders. However, the use of TZDs has been linked to adverse effects, such as weight gain and fluid retention, highlighting the need for a deeper understanding of PPARγ function and regulation. Recent advances in recombinant protein technology have enabled the production of PPARγ in substantial quantities, facilitating detailed biochemical and structural studies. Research into the binding interactions of PPARγ with its ligands and co-regulators is essential for the development of novel therapeutic agents that can selectively modulate its activity, potentially minimizing side effects while maximizing metabolic benefits. This growing body of knowledge not only contributes to our understanding of PPARγ's role in metabolism but also opens new avenues for targeted drug design and the treatment of related metabolic conditions.

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