|Other Names||Methylglutaconyl-CoA hydratase, mitochondrial, AU-specific RNA-binding enoyl-CoA hydratase, AU-binding protein/enoyl-CoA hydratase, AUH|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Catalyzes the conversion of 3-methylglutaconyl-CoA to 3- hydroxy-3-methylglutaryl-CoA. Has very low enoyl-CoA hydratase activity. Was originally identified as RNA-binding protein that binds in vitro to clustered 5'-AUUUA-3' motifs.|
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Provided below are standard protocols that you may find useful for product applications.
The methylglutaconyl-CoA hydratase, mitochondrial proteinbinds to the AU-rich element (ARE), a common element found in the3' UTR of rapidly decaying mRNA such as c-fos, c-myc andgranulocyte/ macrophage colony stimulating factor. ARE elements areinvolved in directing RNA to rapid degradation and deadenylation.AUH is also homologous to enol-CoA hydratase, an enzyme involved infatty acid degradation, and has been shown to have intrinsichydratase enzymatic activity. AUH is thus a bifunctional chimerabetween RNA binding and metabolic enzyme activity. A possiblesubcellular localization in the mitochondria has been demonstratedfor the mouse homolog of this protein which shares 92% identitywith the human protein. It has been suggested that AUH may have anovel role as a mitochondrial located AU-binding protein. Human AUHis expressed as a single mRNA species of 1.8 kb, and translated asa 40-kDa precursor protein which is subsequently processed to a32-kDa mature form.
Kurimoto, K., et al. Proteins 75(2):360-372(2009)Vieira, A.R., et al. Genet. Med. 10(9):668-674(2008)Mack, M., et al. FEBS J. 273(9):2012-2022(2006)Illsinger, S., et al. Pediatr. Neurol. 30(3):213-215(2004)Ly, T.B., et al. Hum. Mutat. 21(4):401-407(2003)
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