Analytical Data
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Gene name
CYP1A2
- Application
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Alternative Names
CYP1A2；Cytochrome P450 1A2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05177
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Expression Region
2-516aa
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AA Sequence
ALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLSDRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPELWEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLEFSVPPGVKVDLTPIYGLTMKHARCEHVQARLRFSIN
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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
CYP1A2 is a member of the cytochrome P450 family of enzymes, which play a crucial role in the metabolism of various xenobiotics and endogenous compounds. This enzyme is primarily expressed in the liver and is responsible for the oxidative metabolism of many drugs, dietary components, and environmental chemicals. CYP1A2 is noted for its involvement in the bioactivation of procarcinogens and the metabolism of caffeine, making it significant in pharmacogenetics and toxicology studies. Research on recombinant CYP1A2 proteins has gained momentum due to the enzyme's complex mechanisms and its variations in activity among individuals, influenced by genetic polymorphisms and environmental factors. Expressing CYP1A2 in a recombinant system allows for detailed characterization of its catalytic properties, substrate specificity, and interactions with inhibitors or activators. These studies contribute to our understanding of drug metabolism variability and help identify potential drug-drug interactions, ultimately aiding in the development of tailored therapeutic strategies. Additionally, the recombinant proteins serve as valuable tools for screening and assessing the safety of new pharmaceuticals and environmental compounds, fostering advances in both clinical and regulatory science. The continued research efforts on CYP1A2 will enhance our understanding of its biological roles and implications in health and disease, supporting the advancement of precision medicine.
