Anti-NADPH oxidase 1 NOX1 Antibody Picoband® Fluoro488 Conjugated

NOX1 (NADPH OXIDASE 1), also known as NOH1, MOX1 or GP91-2, is an enzyme that in humans is encoded by the NOX1 gene. It is also a homolog of the catalytic subunit of the superoxide-generating NADPH oxidase of phagocytes, gp91phox. The NOX1 gene is mapped to Xq22.1. NOX1 was expressed in colon, prostate, uterus, and vascular smooth muscle, but not in peripheral blood leukocytes. The deduced 564-amino acid NOX1 protein, which is 58% identical to CYBB, contains 6 membrane-spanning regions, conserved flavin and pyridine nucleotide-binding sites, and histidines possibly involved in heme ligation. Overexpression of MOX1 in NIH 3T3 cells increased superoxide generation and cell growth. Cells expressing MOX1 had a transformed appearance, showed anchorage-independent growth, and produced tumors in athymic mice. Disruption of either Nox1 or Nox2 significantly delayed progression of motor neuron disease in these mice. However, 50% survival rates were enhanced significantly more by Nox2 deletion than Nox1 deletion.

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.

Adaptive Immunity, Cancer, Cell Biology, Channels, DNA/RNA, DNA Damage & Repair, DNA Damage Response, Epigenetics and Nuclear Signaling, Immunology, Metabolic Signaling Pathways, Metabolism, Nucleotide Metabolism, Oxidative Stress, Pathways and Processes, Plasma Membrane, Redox Metabolism, Signal Transduction, T Cells

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.

1. Banfi, B., Maturana, A., Jaconi, S., Arnaudeau, S., Laforge, T., Sinha, S., Ligeti, E., Demaurex, N., Krause, K.-H. A mammalian H+ channel generated through alternative splicing of the NADPH oxidase homolog NOH-1. Science 287: 138-141, 2000. 2. Behrens, M. M., Ali, S. S., Dao, D. N., Lucero, J., Shekhtman, G., Quick, K. L., Dugan, L. L. Ketamine-induced loss of phenotype of fast-spiking interneurons is mediated by NADPH-oxidase. Science 318: 1645-1647, 2007. 3. Lachgar A, Sojic N, Arbault S, et al. (1999) . Amplification of the inflammatory cellular redox state by human immunodeficiency virus type 1-immunosuppressive tat and gp160 proteins.