Date published: 2026-5-7

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CYP4A11 Substrates

Santa Cruz Biotechnology now offers a broad range of CYP4A11 Substrates for use in various applications. CYP4A11 substrates are crucial tools in the study of the cytochrome P450 4A11 enzyme, which is part of the broader cytochrome P450 family involved in the metabolism of fatty acids and other endogenous substrates. CYP4A11 is particularly important in the hydroxylation of medium-chain fatty acids, such as lauric acid, and plays a significant role in the regulation of blood pressure and kidney function through its involvement in the metabolism of arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE). By using CYP4A11 substrates, researchers can monitor the enzyme's activity and investigate its role in various physiological and pathological processes. These substrates are extensively used in studies aimed at understanding the enzyme's function in lipid metabolism, cardiovascular health, and the development of hypertension. The ability to measure CYP4A11 activity with specific substrates allows scientists to explore the enzyme's contribution to metabolic pathways and to study how genetic variations in CYP4A11 may influence individual susceptibility to diseases. These substrates are indispensable for advancing research in toxicology and metabolic diseases. View detailed information on our available CYP4A11 Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Lauric Acid

143-07-7sc-205367
sc-205367A
sc-205367B
25 g
100 g
250 g
$31.00
$36.00
$79.00
1
(0)

Lauric Acid interacts with CYP4A11 through its long hydrocarbon chain, which enhances hydrophobic interactions with the enzyme's active site. This fatty acid exhibits unique conformational dynamics that can influence the enzyme's substrate accessibility. Its presence can alter the enzyme's catalytic efficiency, potentially affecting lipid metabolism pathways. Additionally, the acid's ability to form micelles may impact local concentration gradients, further influencing enzymatic reactions.