Analytical Data
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Gene name
FMO1
- Application
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Alternative Names
Dimethylaniline oxidase 1; Fetal hepatic flavin-containing monooxygenase 1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q01740
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Expression Region
Ala2~Leu271
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Molecular Weight
34kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
Related Products
Protein Description
FMO1 (Flavin-containing Monooxygenase 1) is a critical enzyme in the family of flavin-dependent monooxygenases, involved in the metabolism of various endogenous and exogenous substrates, including drugs and xenobiotics. The study of FMO1 has gained significant attention due to its role in drug metabolism, detoxification processes, and individual variability in drug responses, which can lead to adverse drug reactions. Notably, FMO1 is expressed in various tissues, including the liver, and its activity can be influenced by genetic polymorphisms, disease states, and environmental factors. The recombinant production of FMO1 has become essential for elucidating its enzymatic mechanisms and substrate specificity, facilitating high-throughput screening in drug discovery. Furthermore, understanding the structural and functional properties of FMO1 is crucial for designing better therapeutic agents and predicting drug interactions. Recent advances in recombinant DNA technology and protein purification methods have enabled researchers to produce large quantities of active FMO1, fostering studies that explore its role in metabolism and the potential implications for personalized medicine. Overall, FMO1 recombinant protein research provides insights into the complexities of human metabolism and the impact of genetic diversity on pharmacotherapy.
