EPHX1 Human
Description
EPHX1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 451 amino acids (21-455a.a) and having a molecular mass of 52.2kDa.
EPHX1 is fused to a 16 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Epoxide Hydrolase 1 (EH1), also known as microsomal epoxide hydrolase (mEH) or EPHX1, is an enzyme that plays a crucial role in the metabolism of both xenobiotic and endogenous epoxides. This enzyme is part of the hydrolase family and is involved in the detoxification processes within the body. The recombinant form of this enzyme, produced through genetic engineering techniques, is used extensively in research and therapeutic applications.
mEH is a membrane-bound enzyme found in the endoplasmic reticulum of cells. It catalyzes the hydrolysis of epoxides to their corresponding diols, which are less reactive and more water-soluble, facilitating their excretion from the body. This reaction is essential for the detoxification of harmful compounds, including those derived from environmental pollutants, drugs, and endogenous metabolic processes .
The EPHX1 gene, located on chromosome 1q42.1, encodes the mEH enzyme. Several polymorphisms in this gene have been identified, which can affect the enzyme’s activity. For instance, the His139Arg polymorphism has been associated with variations in enzyme activity and susceptibility to certain diseases . These genetic variations can influence an individual’s response to environmental toxins and their risk of developing conditions such as cancer, preeclampsia, and neurological disorders .
While mEH is primarily known for its role in xenobiotic metabolism, it also has significant endogenous functions. It metabolizes epoxides derived from fatty acids, such as epoxyeicosatrienoic acids (EETs), which are involved in various physiological processes, including inflammation and cardiovascular regulation . The enzyme’s activity can influence the levels of these bioactive lipids, thereby impacting cardiovascular health and disease .
The recombinant form of mEH is produced using human cells or other expression systems to ensure it closely mimics the natural enzyme. This recombinant enzyme is used in various research applications, including the study of drug metabolism, toxicology, and the development of therapeutic interventions. For example, recombinant mEH is utilized in enzyme-linked immunosorbent assays (ELISAs) to quantify the enzyme’s levels in biological samples, aiding in the diagnosis and monitoring of diseases .
