Analytical Data
-
Gene name
FMO3
- Application
-
Alternative Names
FMO3;Flavin-containing monooxygenase 3
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P31513
-
Expression Region
1-408aa
-
AA Sequence
MGKKVAIIGAGVSGLASIRSCLEEGLEPTCFEKSNDIGGLWKFSDHAEEGRASIYKSVFSNSSKEMMCFPDFPFPDDFPNFMHNSKIQEYIIAFAKEKNLLKYIQFKTFVSSVNKHPDFATTGQWDVTTERDGKKESAVFDAVMVCSGHHVYPNLPKESFPGLNHFKGKCFHSRDYKEPGVFNGKRVLVVGLGNSGCDIATELSRTAEQVMISSRSGSWVMSRVWDNGYPWDMLLVTRFGTFLKNNLPTAISDWLYVKQMNARFKHENYGLMPLNGVLRKEPVFNDELPASILCGIVSVKPNVKEFTETSAIFEDGTIFEGIDCVIFATGYSFAYPFLDESIIKSRNNEIILFKGVFPPLLEKSTIAVIGFVQSLGAAIPTVDLQSRWAAQVIKGTCTLPSMEDMMND
-
Molecular Weight
51.6 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
-
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
Related Products
Protein Description
FMO3 (Flavin-containing monooxygenase 3) is a key enzyme involved in the metabolism of various xenobiotics and endogenous compounds, contributing significantly to drug metabolism and the detoxification processes in the liver. The study of FMO3 is particularly important due to its role in the bioactivation and deactivation of drugs, as well as its involvement in the metabolism of dietary substances and environmental chemicals. Mutations in the FMO3 gene can lead to Trimethylaminuria (TMAU), a disorder characterized by the accumulation of trimethylamine, resulting in distinct bodily odors. Understanding the structure, function, and regulatory mechanisms of FMO3 through the development of recombinant proteins has become crucial in pharmacogenomics and personalized medicine. The recombinant version of FMO3 allows for detailed biochemical studies to elucidate its catalytic mechanisms and substrate specificity, as well as its interaction with various ligands. Additionally, investigating FMO3's role in different populations and its polymorphisms can provide insights into variations in drug response and susceptibility to toxic compounds. Overall, research into FMO3 recombinant protein not only enhances our understanding of metabolic processes but also opens avenues for therapeutic interventions and the development of better drug formulations.











