Analytical Data
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Gene name
CYP2F2
- Application
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Alternative Names
CYPIIF2; Cytochrome P450-NAH-2; Naphthalene dehydrogenase; Naphthalene hydroxylase
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Species
Mouse
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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
P33267
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Expression Region
Arg25-Arg491
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Molecular Weight
57kDa
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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
CYP2F2 is a member of the cytochrome P450 enzyme family, which plays a crucial role in the metabolism of various endogenous and exogenous compounds, including drugs, steroids, and environmental toxins. It is primarily expressed in the lungs and is implicated in the biotransformation of nicotine and other xenobiotics. Research into CYP2F2 is vital due to its potential impact on drug metabolism and toxicology, particularly in understanding individual responses to medications and the risks associated with exposure to airborne pollutants. The study of CYP2F2 recombinant proteins allows scientists to investigate its functional properties, substrate specificity, and interactions with various inhibitors or inducers. This understanding can lead to advancements in personalized medicine, where genetic variations in CYP2F2 may influence therapeutic outcomes. Furthermore, elucidating the biochemical pathways involving CYP2F2 can provide insights into the pharmacokinetics of substances that undergo metabolism by this enzyme, thereby enhancing drug safety and efficacy. The recombinant expression of CYP2F2 also paves the way for the development of novel therapeutic agents and can aid in the design of more effective drug formulations by predicting metabolic pathways and interactions. Overall, the research on CYP2F2 recombinant proteins holds significant promise for improving health outcomes and understanding metabolic processes in human physiology.
