Cat: IPD-X38670

Recombinant Human PON3 Protein,His

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Analytical Data

  • Gene name

    PON3

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Serum paraoxonase/lactonase 3

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q15166

  • Expression Region

    Gly2~Leu354

  • Molecular Weight

    86/43kDa

  • 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.

Quality inspection process

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Protein Description

PON3, or paraoxonase 3, is a member of the paraoxonase family of enzymes, which play a crucial role in lipid metabolism and antioxidant defense. Unlike its closely related homologues, PON1 and PON2, PON3 is predominantly found in the extracellular space, particularly in high-density lipoproteins (HDL). It has been implicated in various physiological processes, including the hydrolysis of toxic organophosphates and the prevention of oxidative stress, which contributes to atherogenesis and other cardiovascular diseases. Research has indicated that PON3 may have protective effects against the development of atherosclerosis and other inflammatory conditions. Given the rising prevalence of cardiovascular diseases, understanding the role of PON3 in lipid metabolism and its potential as a therapeutic target has garnered significant interest in the scientific community. Additionally, the study of PON3 recombinant proteins allows for the exploration of its enzymatic activity and interactions with various substrates, providing insights into its structural-function relationship and potential applications in medicine. Advances in biotechnology have facilitated the production and characterization of PON3, paving the way for further investigations into its role in disease and its utility in therapeutic settings. Understanding the molecular mechanisms by which PON3 operates will enhance our knowledge of cardiovascular health and may lead to new strategies for disease prevention and management.

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