sEH is widely expressed in mammalian cells as a cytosolic enzyme where it primarily serves the function of converting epoxyeicosatrienoic acids (EETs), epoxyeicosatetraenoic acids (EPAs), and epoxydocosapentaenoic acids (DPAs) to their corresponding diols, thereby limiting or ending their cell signaling actions; in this capacity, sEH appears to play a critical in vivo role in limiting the effects of these epoxides in animal models and possibly humans. However, sEH also metabolizes the epoxides of linoleic acid viz., Vernolic acid (leukotoxins) and Coronaric acids (isoleukotoxins) to their corresponding diols which are highly toxic in animal models and possibly humans (see Vernolic acid#toxicity, Coronaric acid#toxicity, and soluble epoxide hydrolase). sEH also possesses hepoxilin-epoxide hydrolase activity, converting bioactive hepoxilins to their inactive trioxilin products (see below section "Hepoxilin-epoxide hydrolase").