Date published: 2026-5-28

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CYP1A2 Substrates

Santa Cruz Biotechnology now offers a broad range of CYP1A2 Substrates for use in various applications. CYP1A2, part of the cytochrome P450 enzyme family, is crucial in the metabolism of various endogenous and exogenous compounds, including hormones, fatty acids, and xenobiotics such as drugs and environmental toxins. CYP1A2 Substrates are vital tools in scientific research, providing the means to study this enzyme's activity, substrate specificity, and role in metabolic pathways. Researchers use these substrates to investigate how CYP1A2 metabolizes specific compounds, facilitating the exploration of enzyme kinetics, identification of metabolic intermediates, and understanding of how this enzyme influences the detoxification and bioactivation of chemicals within the body. These substrates are commonly employed in biochemical assays to assess the catalytic efficiency of CYP1A2, offering insights into its role in the metabolism of compounds such as caffeine, acetaminophen, and polycyclic aromatic hydrocarbons (PAHs). Furthermore, CYP1A2 Substrates are valuable in toxicology and pharmacokinetics research, where they help explain the impact of CYP1A2-mediated metabolism on drug efficacy, safety, and the formation of potentially harmful metabolites. The availability of these substrates has significantly advanced research in fields like biochemistry, molecular biology, and environmental science, providing researchers with essential tools to dissect the complex interactions between CYP1A2 and its substrates. By offering a deeper understanding of the metabolic processes mediated by CYP1A2, these substrates are indispensable for advancing our knowledge of how this enzyme regulates biochemical pathways and maintains cellular homeostasis. View detailed information on our available CYP1A2 Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Phenacetin

62-44-2sc-257998
sc-257998A
50 g
250 g
$48.00
$91.00
3
(0)

Phenacetin exhibits unique interactions with CYP1A2, primarily through hydrogen bonding and hydrophobic interactions that enhance substrate affinity. Its aromatic structure allows for effective π-π interactions, influencing the enzyme's conformational dynamics. The compound's metabolic pathway is characterized by its biotransformation, which can generate reactive metabolites, potentially impacting downstream signaling pathways. This behavior underscores its role in modulating enzymatic activity and metabolic flux.

(R)-(+)-Warfarin

5543-58-8sc-255498
5 mg
$627.00
(0)

(R)-(+)-Warfarin interacts with CYP1A2 through specific steric and electronic effects, facilitating its metabolism. The compound's chiral nature influences binding affinity, leading to distinct enantioselective pathways. Its planar structure promotes π-π stacking interactions, which can stabilize enzyme-substrate complexes. The reaction kinetics reveal a complex interplay of competitive inhibition and allosteric modulation, affecting the overall metabolic profile and influencing the enzyme's catalytic efficiency.