PHOME | 1028430-42-3

PHOME (p-hydroxymercuribenzoic acid) is a fluorogenic substrate specifically designed to measure the activity of human soluble epoxide hydrolase (sEH), an enzyme involved in the metabolism of bioactive lipids. PHOME contains a fluorophore that releases fluorescence upon enzymatic hydrolysis by sEH, allowing for real-time monitoring of enzyme activity. This substrate is highly stable in aqueous solutions, making it suitable for a variety of experimental conditions.

One of the primary applications of PHOME is in the monitoring of sEH activity in enzyme assays. The substrate’s ability to produce a measurable fluorescence signal upon cleavage by sEH provides a simple and effective method to quantify the enzyme's activity. This capability is crucial for understanding the role of sEH in various physiological processes, including inflammation, blood pressure regulation, and lipid signaling. By using PHOME, researchers can gain insights into how sEH modulates the activity of epoxyeicosatrienoic acids (EETs) and other related lipid mediators.

Another significant application of PHOME is in high throughput screening (HTS) programs. Due to its stable nature in aqueous solutions and the rapid, easily quantifiable fluorescence signal, PHOME is ideal for screening large libraries of potential sEH inhibitors. This is particularly useful in drug discovery programs aimed at identifying new therapeutic agents for diseases associated with sEH dysregulation, such as cardiovascular disease, neurological disorders, and inflammation. PHOME facilitates efficient and cost-effective screening of compounds that may modulate sEH activity.

PHOME is also utilized in pharmacological studies investigating the effects of sEH inhibitors. By tracking changes in fluorescence levels, researchers can assess the efficacy of various small molecules or biologics in inhibiting sEH activity. This application is valuable in evaluating the potential of sEH inhibitors as therapeutic agents, particularly in conditions where inhibiting sEH may be beneficial, such as reducing hypertension or alleviating inflammation. The ability to monitor enzyme activity in real-time allows for more precise and dynamic studies of drug interactions with sEH.

Finally, PHOME plays a role in the study of epoxide hydrolase enzymes in general, particularly for comparative studies across different species or in different tissues. Since PHOME is a substrate for human sEH, it can be used in cross-species studies to compare enzyme activity in human tissues versus animal models. This allows for a better understanding of species-specific differences in sEH function, which can be crucial for designing more effective therapies. Additionally, the use of PHOME in studying sEH in tissue-specific contexts helps unravel the enzyme's role in localized biochemical processes.