|Application ||IHC-P, WB, E|
|Calculated MW||57611 Da|
|Antigen Region||156-183 aa|
|Other Names||Cytochrome P450 2J2, Arachidonic acid epoxygenase, CYPIIJ2, CYP2J2|
|Target/Specificity||This CYP2J2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 156-183 amino acids from the Central region of human CYP2J2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CYP2J2 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Metabolizes arachidonic acid predominantly via a NADPH- dependent olefin epoxidation to all four regioisomeric cis- epoxyeicosatrienoic acids. One of the predominant enzymes responsible for the epoxidation of endogenous cardiac arachidonic acid pools (PubMed:8631948). Catalyzes the monooxygenation of a various compounds, such as danazol, amiodarone, terfenadine, astemizole, thioridazine, tamoxifen, cyclosporin A and nabumetone (PubMed:19923256). Catalyzes hydroxylation of the anthelmintics albendazole and fenbendazole (PubMed:23959307). Catalyzes the sulfoxidation of fenbedazole (PubMed:19923256).|
|Cellular Location||Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein|
|Tissue Location||Highly expressed in heart, present at lower levels in liver, ileum, jejunum, colon, and kidney|
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Provided below are standard protocols that you may find useful for product applications.
CYP2J2 is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and is thought to be the predominant enzyme responsible for epoxidation of endogenous arachidonic acid in cardiac tissue.
Wu S., Moomaw C.R., Tomer K.B.J. Biol. Chem. 271:3460-3468(1996)
King L.M., Ma J., Srettabunjong S.Mol. Pharmacol. 61:840-852(2002)
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