Anti-NADPH oxidase 4/NOX4 Antibody Picoband® Fluoro647 Conjugated

NADPH oxidase 4 is an enzyme that in humans is encoded by the NOX4 gene, and is a member of the NOX family of NADPH oxidases. This gene encodes a member of the NOX-family of enzymes that functions as the catalytic subunit the NADPH oxidase complex. The encoded protein is localized to non-phagocytic cells where it acts as an oxygen sensor and catalyzes the reduction of molecular oxygen to various reactive oxygen species (ROS) . The ROS generated by this protein have been implicated in numerous biological functions including signal transduction, cell differentiation and tumor cell growth. A pseudogene has been identified on the other arm of chromosome 11. Alternative splicing results in multiple transcript variants.

A synthetic peptide corresponding to a sequence at the C-terminus of human NADPH oxidase 4, which shares 97.2% amino acid (aa) sequence identity with both mouse and rat NADPH oxidase 4.

Expressed by distal tubular cells in kidney cortex and in endothelial cells (at protein level) . Widely expressed. Strongly expressed in kidney and to a lower extent in heart, adipocytes, hepatoma, endothelial cells, skeletal muscle, brain, several brain tumor cell lines and airway epithelial cells.

Atherosclerosis, Cardiovascular, Cell Biology, Drug Metabolism, Heart Disease, Metabolic Signaling Pathways, Metabolism, Oxidative Stress, Pathways and Processes, Redox Metabolism, Signal Transduction, Vascular Inflammation

Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation. Isoform 3 is not functional. Isoform 5 and isoform 6 display reduced activity.

1. Ago, T., Kitazono, T., Ooboshi, H., Iyama, T., Han, Y. H., Takada, J., Wakisaka, M., Ibayashi, S., Utsumi, H., Iida, M. Nox4 as the major catalytic component of an endothelial NAD (P) H oxidase. Circulation 109: 227-233, 2004. 2. Geiszt, M., Kopp, J. B., Varnai, P., Leto, T. L. Identification of Renox, an NAD (P) H oxidase in kidney. Proc. Nat. Acad. Sci. 97: 8010-8014, 2000. 3. Shiose, A., Kuroda, J., Tsuruya, K., Hirai, M., Hirakata, H., Naito, S., Hattori, M., Sakaki Y., Sumimoto, H. A novel superoxide-producing NAD (P) H oxidase in kidney. J. Biol. Chem. 276: 1417-1423, 2001.