EPHX2 Protein, Human (sf9, His)

EPHX2 Protein, a bifunctional enzyme, displays epoxide hydrolase activity in its C-terminal domain, crucial for xenobiotic metabolism. It degrades toxic epoxides and influences steady-state levels of physiological mediators. The N-terminal domain exhibits lipid phosphatase activity, prioritizing threo-9,10-phosphonooxy-hydroxy-octadecanoic acid. EPHX2's multifaceted enzymatic activities underscore its diverse roles in cellular processes, including xenobiotic metabolism and lipid homeostasis. EPHX2 Protein, Human (sf9, His) is the recombinant human-derived EPHX2 protein, expressed by Sf9 insect cells, with N-His labeled tag. The total length of EPHX2 Protein, Human (sf9, His) is 555 a.a., with molecular weight of ~65 kDa.

The EPHX2 protein is a bifunctional enzyme with distinct activities in its C-terminal and N-terminal domains. The C-terminal domain exhibits epoxide hydrolase activity, acting on both alkene oxides and arene oxides. This functionality plays a crucial role in xenobiotic metabolism by degrading potentially toxic epoxides and contributes to determining steady-state levels of physiological mediators. On the other hand, the N-terminal domain of EPHX2 possesses lipid phosphatase activity, displaying the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, and 12-phosphonooxy-octadec-9E-enoic acid. Additionally, it exhibits phosphatase activity toward lyso-glycerophospholipids, with some lower activity observed toward lysolipids of sphingolipid and isoprenoid phosphates. These multifaceted enzymatic activities highlight the diverse roles of EPHX2 in cellular processes, including xenobiotic metabolism and lipid homeostasis.

Human

Sf9 insect cells

N-His

P34913 (M1-M555)

2053  [NCBI]

Approximately 65 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.