SEH / EPHX2 Antibody (C-Terminus)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| IHC-P, E |
---|---|
Primary Accession | P34913 |
Reactivity | Human, Monkey |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 63kDa |
Dilution | IHC-P (5-10 µg/ml) |
Gene ID | 2053 |
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Other Names | Bifunctional epoxide hydrolase 2, Cytosolic epoxide hydrolase 2, CEH, 3.3.2.10, Epoxide hydratase, Soluble epoxide hydrolase, SEH, Lipid-phosphate phosphatase, 3.1.3.76, 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. |
Name | EPHX2 (HGNC:3402) |
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Function | Bifunctional enzyme (PubMed:12574510). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12574510, PubMed:12869654, PubMed:22798687). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady- state levels of physiological mediators (PubMed:12574510, PubMed:12869654, PubMed:21217101, PubMed:22798687). |
Cellular Location | Cytoplasm. Peroxisome. |
Volume | 50 µl |

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Background
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.
References
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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