Date published: 2026-5-5

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CYP2B6 Substrates

Santa Cruz Biotechnology now offers a broad range of CYP2B6 Substrates for use in various applications. CYP2B6 is an important member of the cytochrome P450 enzyme family, playing a crucial role in the metabolism of a wide range of endogenous and exogenous compounds, including steroids, fatty acids, and environmental chemicals. CYP2B6 Substrates are essential tools in scientific research, enabling researchers to explore the enzyme's activity, substrate specificity, and role in metabolic pathways. These substrates allow scientists to study how CYP2B6 catalyzes the oxidation of various compounds, facilitating the investigation of enzyme kinetics, the identification of metabolic products, and the understanding of how this enzyme contributes to the biotransformation and detoxification processes in cells. CYP2B6 Substrates are widely utilized in biochemical assays to measure the enzyme's catalytic efficiency and to explore the impact of genetic variations, environmental factors, and inhibitors on its activity. Additionally, these substrates are valuable in toxicology research, where they are used to examine how CYP2B6-mediated metabolism influences the formation of reactive intermediates and their potential effects on cellular health. The availability of CYP2B6 Substrates has significantly advanced research in fields such as biochemistry, molecular biology, and environmental science, providing critical tools for dissecting the complex interactions between CYP2B6 and its substrates. By offering insights into the metabolic processes mediated by CYP2B6, these substrates are indispensable for advancing our understanding of how this enzyme regulates key biochemical pathways and maintains cellular homeostasis. View detailed information on our available CYP2B6 Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

(S)-Mephenytoin

70989-04-7sc-200975
sc-200975A
5 mg
25 mg
$142.00
$550.00
14
(1)

(S)-Mephenytoin exhibits notable interactions with CYP2B6, characterized by its chiral center that influences binding dynamics. The presence of the ethyl group enhances hydrophobic interactions, promoting a stable enzyme-substrate complex. Additionally, the compound's stereochemistry plays a crucial role in modulating the enzyme's active site, leading to distinct metabolic pathways. Its unique electronic properties contribute to varied reaction kinetics, impacting overall enzymatic activity and selectivity.

Resorufin pentyl ether

87687-03-4sc-208304
sc-208304A
1 mg
5 mg
$204.00
$632.00
2
(0)

Resorufin pentyl ether demonstrates intriguing interactions with CYP2B6, primarily due to its hydrophobic pentyl chain, which enhances affinity for the enzyme's active site. This compound's unique electronic structure facilitates electron transfer processes, influencing the rate of metabolic reactions. The ether functionality allows for specific hydrogen bonding, further stabilizing enzyme-substrate complexes. Its distinct steric properties can modulate substrate accessibility, affecting overall catalytic efficiency and selectivity in metabolic pathways.

7-Ethoxycoumarin

31005-02-4sc-207170
sc-207170A
25 mg
100 mg
$41.00
$71.00
(0)

7-Ethoxycoumarin exhibits notable characteristics when interacting with CYP2B6, primarily through its ethoxy group, which enhances solubility and promotes favorable binding interactions. The compound's planar structure allows for effective π-π stacking with aromatic residues in the enzyme, influencing binding affinity. Additionally, its unique electron-donating properties can alter the redox state of the enzyme, impacting reaction kinetics and metabolic stability. The compound's conformational flexibility may also play a role in modulating enzyme activity and substrate turnover.

(R)-Mephenytoin

71140-51-7sc-215780
10 mg
$260.00
(0)

(R)-Mephenytoin demonstrates intriguing interactions with CYP2B6, primarily due to its chiral center, which influences stereoselectivity in metabolic pathways. The compound's hydrophobic regions facilitate strong van der Waals interactions with the enzyme's active site, enhancing binding efficiency. Its unique electronic configuration can modulate the enzyme's catalytic activity, while the presence of specific functional groups may affect substrate recognition and turnover rates, leading to distinct metabolic profiles.