|Other Names||NADPH oxidase organizer 1, NADPH oxidase regulatory protein, Nox organizer 1, Nox-organizing protein 1, SH3 and PX domain-containing protein 5, NOXO1, P41NOX, SH3PXD5|
|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||Constitutively potentiates the superoxide-generating activity of NOX1 and NOX3 and is required for the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity. Isoform 3 is more potent than isoform 1 in activating NOX3. Together with NOXA1, may also substitute to NCF1/p47phox and NCF2/p67phox in supporting the phagocyte NOX2/gp91phox superoxide-generating activity.|
|Cellular Location||Isoform 3: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Isoform 3 associates with the plasma membrane in a lipid-dependent manner (PubMed:12716910)|
|Tissue Location||Expressed in testis, small and large intestines, liver, kidney and pancreas. Isoform 3 is mainly expressed in colon. Isoform 1 is preferentially expressed in testis.|
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Provided below are standard protocols that you may find useful for product applications.
NADPH oxidases (NOXs) catalyze the transfer of electronsfrom NADPH to molecular oxygen to generate reactive oxygen species(ROS). NOX organizers, such as NOXO1, target NOX activators (seeNOXA1; MIM 611255) to NOX and also target NOX to differentsubcellular compartments (Opitz et al., 2007 [PubMed17189823]).
Dutta, S., et al. PLoS ONE 5 (5), E10478 (2010) :Opitz, N., et al. Free Radic. Biol. Med. 42(2):175-179(2007)Yamamoto, A., et al. Biochem. Biophys. Res. Commun. 352(2):560-565(2007)Takeya, R., et al. FEBS J. 273(16):3663-3677(2006)Cheng, G., et al. J. Biol. Chem. 281(26):17718-17726(2006)
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