|Application ||WB, IHC-P, IF, E|
|Calculated MW||74424 Da|
|Other Names||Peroxisomal acyl-coenzyme A oxidase 1, AOX, Palmitoyl-CoA oxidase, Straight-chain acyl-CoA oxidase, SCOX, ACOX1, ACOX|
|Target/Specificity||This ACOX1 monoclonal antibody is generated from mouse immunized with ACOX1 recombinant protein.|
|Format||Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, 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||ACOX1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Catalyzes the desaturation of acyl-CoAs to 2-trans- enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 2 is twice as active as isoform 1 against 16-hydroxy- palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl- CoA.|
|Tissue Location||Widely expressed with highest levels of isoform 1 and isoform 2 detected in testis. Isoform 1 is expressed at higher levels than isoform 2 in liver and kidney while isoform 2 levels are higher in brain, lung, muscle, white adipose tissue and testis. Levels are almost equal in heart|
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Provided below are standard protocols that you may find useful for product applications.
ACOX1 is the first enzyme of the fatty acid beta-oxidation pathway, which catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. It donates electrons directly to molecular oxygen, thereby producing hydrogen peroxide. Defects in this gene result in pseudoneonatal adrenoleukodystrophy, a disease that is characterized by accumulation of very long chain fatty acids.
Lu, Y., et al. J. Lipid Res. 49(12):2582-2589(2008) Carrozzo, R., et al. Am. J. Med. Genet. A 146A (13), 1676-1681 (2008) Omi, S., et al. J. Biochem. 143(5):649-660(2008)
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