|Other Names||NADPH oxidase 1, NOX-1, 1---, Mitogenic oxidase 1, MOX-1, NADH/NADPH mitogenic oxidase subunit P65-MOX, NOH-1, NOX1, MOX1, NOH1|
|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||NOH-1S is a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues. It participates in the regulation of cellular pH and is blocked by zinc. NOH-1L is a pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H(+) ions as part of its electron transport mechanism, whereas NOH-1S does not contain an electron transport chain.|
|Cellular Location||Cell projection, invadopodium membrane; Multi-pass membrane protein|
|Tissue Location||NOH-1L is detected in colon, uterus, prostate, and colon carcinoma, but not in peripheral blood leukocytes. NOH- 1S is detected only in colon and colon carcinoma cells|
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Provided below are standard protocols that you may find useful for product applications.
Voltage-gated proton (hydrogen) channels play an importantrole in cellular defense against acidic stress. They are uniqueamong ion channels with respect to their extremely highselectivity, marked temperature dependence, and unitaryconductance, which is 3 orders of magnitude lower than that of mostother ion channels. NOX1 is a homolog of the catalytic subunit ofthe superoxide-generating NADPH oxidase of phagocytes, gp91phox.Two transcript variants encoding different isoforms have been foundfor this gene.
Sancho, P., et al. J. Biol. Chem. 285(32):24815-24824(2010)van Bruggen, R., et al. Blood 115(26):5398-5400(2010)Roberts, K.E., et al. Gastroenterology 139(1):130-139(2010)Malec, V., et al. Free Radic. Biol. Med. 48(12):1626-1635(2010)Manea, A., et al. Biochem. Biophys. Res. Commun. 396(4):901-907(2010)
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