|Application ||WB, IHC-P, IF, E|
|Other Accession||NP_008983, 148536873|
|Calculated MW||Predicted: 62 kDa |
Observed: 64 kDa
|Application Notes||NOX1 antibody can be used for detection of NOX1 by Western blot at 1 - 2 µg/ml. Antibody can also be used for Immunohistochemistry starting at 5 µg/mL. For immunofluorescence start at 20 µg/mL.|
|Target/Specificity||NOX1; NOX1 antibody is human specific.|
|Reconstitution & Storage||NOX1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.|
|Precautions||NOX1 Antibody is for research use only and 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. Cell membrane|
|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 important role in cellular defense against acidic stress (1). NOX1 is a homolog of the catalytic subunit of the superoxide-generating NADPH oxidase of phagocytes, gp91phox (1). Three splice variants of NOX1 have been identified, NOH-1L, NOH-1S and NOH-1Lv (2). NOH-1S is a voltage-gated proton channel that 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 (1-3). NOX1 have the potential to be effective treatments for a range of ischemic diseases (4).
Helmcke I, Heumuller S, Tikkanen R, et al. Identification of structural elements in Nox1 and Nox4 controlling localization and activity. Antioxid. Redox Signal. 2009; 11:1279-87.
Piccoli C, D'Aprile A, Ripoli M, et al. Bone-marrow derived hematopoietic stem/progenitor cells express multiple isoforms of NADPH oxidase and produce constitutively reactive oxygen species. Biochem. Biophys. Res. Commun. 2007; 353:965-72.
Lee JG, Lim EJ, Park DW, et al. A combination of Lox-1 and Nox1 regulates TLR9-mediated foam cell formation. Cell Signal. 2008; 20:2266-75.
Stanic B, Katsuyama M, and Miller FJ Jr. An oxidized extracellular oxidation-reduction state increases Nox1 expression and proliferation in vascular smooth muscle cells via epidermal growth factor receptor activation. Arterioscler. Thromb. Vasc. Biol. 2010; 30:2234-41.
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