|Application ||IHC-P, E|
|Dilution||IHC-P (5-10 µg/ml)|
|Other Names||Bifunctional epoxide hydrolase 2, Cytosolic epoxide hydrolase 2, CEH, 126.96.36.199, Epoxide hydratase, Soluble epoxide hydrolase, SEH, Lipid-phosphate phosphatase, 188.8.131.52, EPHX2|
|Target/Specificity||Human EPHX2. BLAST analysis of the peptide immunogen showed no homology with other human proteins.|
|Reconstitution & Storage||Long term: -70°C; Short term: +4°C|
|Precautions||SEH / EPHX2 Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Bifunctional enzyme (PubMed:12574510). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12869654, PubMed:12574510, PubMed:22798687). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (PubMed:12869654, PubMed:12574510, PubMed:22798687). The N-terminal domain has lipid phosphatase activity, with 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 (PubMed:12574510).|
|Cellular Location||Cytoplasm. Peroxisome.|
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Provided below are standard protocols that you may find useful for product applications.
Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with 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, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate.
Beetham J.K.,et al.Arch. Biochem. Biophys. 305:197-201(1993).
Sandberg M.,et al.Biochem. Biophys. Res. Commun. 221:333-339(1996).
Sandberg M.,et al.J. Biol. Chem. 275:28873-28881(2000).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
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