Cat: IPD-X39044

Recombinant Human FMO3 Protein,His

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Analytical Data

  • Gene name

    FMO3

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Trimethylamine monooxygenase; Hepatic flavin-containing monooxygenase 3; Dimethylaniline oxidase 3

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P31513

  • Expression Region

    Lys280~Thr532

  • Molecular Weight

    31kDa

  • 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

The study of the FMO3 (Flavin-containing monooxygenase 3) recombinant protein has gained significant attention due to its crucial role in drug metabolism and regulation of endogenous compounds. FMO3 is part of the flavin-containing monooxygenase enzyme family, which is involved in the oxidation of a wide array of substrates, including pharmaceuticals, dietary components, and environmental toxins. Variability in FMO3 activity among individuals can lead to differences in drug efficacy and toxicity, highlighting its importance in personalized medicine. Genetic polymorphisms, particularly those affecting the FMO3 gene, can influence enzyme function and have been linked to various health conditions, such as trimethylaminuria, where defective FMO3 leads to the accumulation of trimethylamine, resulting in unpleasant body odor. Furthermore, the recombinant expression of FMO3 in heterologous systems allows for in-depth studies of its enzymatic properties, substrate specificity, and interactions with other metabolic pathways. This enables researchers to better understand how FMO3 contributes to metabolic networks and can aid in the development of therapeutics that are tailored to individual metabolic profiles. Overall, the exploration of FMO3 recombinant protein serves not only to elucidate its biochemical functions but also offers potential insights into pharmacogenomics, toxicology, and the development of safer, more effective drugs.

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