CYP2J2 (Cytochrome p450 2J2) Antibody (YA7934)
(Synonyms: CPJ2)Based on 1 Customer Validation
CYP2J2 (Cytochrome p450 2J2) Antibody (YA7934) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to CYP2J2 (Cytochrome p450 2J2).
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, ICC/IF, FC
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Reactivity :
Human
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Formulation:
Spplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
FC
FC: Flow Cytometry
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|---|---|---|---|
| Dilution Ratio | 1:2000-3000 | 1:100-250 | 1:100 |
Product Details
CYP2J2 (Cytochrome p450 2J2) Antibody (YA7934) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to CYP2J2 (Cytochrome p450 2J2).
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman
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Calculated Molecular Weight Predicted band size: 57.4 kDa
Full length human recombinant protein of human CYP2J2 produced in HEK293T cell.
Endogenous
Affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Spplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
CYP2J2 is an A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) in the cardiovascular system. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of PUFA. Converts arachidonic acid to four regioisomeric epoxyeicosatrienoic acids (EpETrE), likely playing a major role in the epoxidation of endogenous cardiac arachidonic acid pools. In endothelial cells, participates in eicosanoids metabolism by converting hydroperoxide species into hydroxy epoxy metabolites. In combination with 15-lipoxygenase metabolizes arachidonic acid and converts hydroperoxyicosatetraenoates (HpETEs) into hydroxy epoxy eicosatrienoates (HEETs), which are precursors of vasodilatory trihydroxyicosatrienoic acids (THETAs). This hydroperoxide isomerase activity is NADPH- and O2-independent. Catalyzes the monooxygenation of a various xenobiotics, such as danazol, amiodarone, terfenadine, astemizole, thioridazine, tamoxifen, cyclosporin A and nabumetone. Catalyzes hydroxylation of the anthelmintics albendazole and fenbendazole. Catalyzes the sulfoxidation of fenbedazole[1][2][3][4][5].
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Subcellular Localization
Endoplasmic reticulum membrane,Microsome membrane
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Expression
Tissue_Specificity: Highly expressed in heart, present at lower levels in liver, kidney and skeletal muscle (at protein level) -
Isoforms & Post-Translational Modification
P51589: 502 amino acids, molecular weight 57611 Da.
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SwissProt ID
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Synonyms
CPJ2
Documentation
References
[1]. Lucas D, et al. Stereoselective epoxidation of the last double bond of polyunsaturated fatty acids by human cytochromes P450. J Lipid Res. 2010 May;51(5):1125-33. [Content Brief]
[2]. Wu S, et al. Molecular cloning and expression of CYP2J2, a human cytochrome P450 arachidonic acid epoxygenase highly expressed in heart. J Biol Chem. 1996 Feb 16;271(7):3460-8. [Content Brief]
[3]. Chawengsub Y, et al. Identification of 13-hydroxy-14,15-epoxyeicosatrienoic acid as an acid-stable endothelium-derived hyperpolarizing factor in rabbit arteries. J Biol Chem. 2009 Nov 6;284(45):31280-90. [Content Brief]
[4]. Lee CA, et al. Identification of novel substrates for human cytochrome P450 2J2. Drug Metab Dispos. 2010 Feb;38(2):347-56. [Content Brief]
[5]. Wu Z, et al. CYP2J2 and CYP2C19 are the major enzymes responsible for metabolism of albendazole and fenbendazole in human liver microsomes and recombinant P450 assay systems. Antimicrob Agents Chemother. 2013 Nov;57(11):5448-56. [Content Brief]