Date published: 2026-5-25

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CYP1A1 Substrates

Santa Cruz Biotechnology now offers a broad range of CYP1A1 Substrates for use in various applications. CYP1A1, a member of the cytochrome P450 enzyme family, plays a critical role in the metabolism of a variety of endogenous and exogenous compounds, including environmental pollutants, drugs, and carcinogens. CYP1A1 Substrates are indispensable tools in scientific research, enabling the detailed study of this enzyme's activity, substrate specificity, and its involvement in metabolic pathways. Researchers use these substrates to investigate how CYP1A1 contributes to the bioactivation or detoxification of compounds, facilitating the exploration of enzyme kinetics, the identification of metabolic products, and the understanding of how this enzyme impacts cellular responses to chemical exposure. These substrates are widely utilized in biochemical assays to assess the catalytic efficiency of CYP1A1, and to study its role in the metabolism of polycyclic aromatic hydrocarbons (PAHs) and other environmental toxins. Additionally, CYP1A1 Substrates are valuable in toxicology research, where they help explain the mechanisms by which CYP1A1-mediated metabolism influences the formation of DNA adducts and the subsequent risk of mutagenesis. The availability of these substrates has significantly advanced research in fields such as biochemistry, toxicology, and environmental science, providing researchers with essential tools to dissect the complex interactions between CYP1A1 and its substrates. By offering insights into the metabolic processes mediated by CYP1A1, these substrates are crucial for advancing our understanding of how this enzyme regulates biochemical pathways and contributes to cellular defense mechanisms. View detailed information on our available CYP1A1 Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

7-Ethoxyresorufin

5725-91-7sc-200606
sc-200606A
2 mg
10 mg
$138.00
$270.00
6
(1)

7-Ethoxyresorufin is a selective substrate for CYP1A1, characterized by its ability to undergo O-deethylation, resulting in the formation of resorufin. This transformation highlights its role in probing cytochrome P450 activity. The compound's electron-rich aromatic system facilitates π-π stacking interactions with the enzyme, enhancing binding efficiency. Additionally, its unique structural features allow for rapid metabolic turnover, making it a valuable tool for studying CYP1A1-mediated biotransformation pathways.