Recombinant Human NADPH oxidase 4 protein
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Recombinant Human NADPH oxidase 4 protein is a Human Full Length protein, in the 1 to 578 aa range, expressed in Cell free, with >85%, suitable for SDS-PAGE.
View Alternative Names
RENOX, NOX4, NADPH oxidase 4, Kidney oxidase-1, Kidney superoxide-producing NADPH oxidase, Renal NAD(P)H-oxidase, KOX-1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human NADPH oxidase 4 protein (AB289740)
SDS-PAGE analysis of ab289740
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
NADPH oxidase 4 plays a role in cellular signaling and oxidative stress responses. The enzyme is part of the NADPH oxidase family which consists of several members each forming complexes with regulatory subunits such as p22phox NOXO1 or NOXA1. These complexes contribute to NOX4's stable and constitutive activity impacting cell growth differentiation and apoptosis processes. Its persistent activation suggests it modulates basal ROS levels acting as a control point in redox-dependent cell signaling.
Pathways
NOX4 is intricately involved in the TGF-beta signaling pathway and the regulation of endothelial nitric oxide synthase (eNOS) activity. The TGF-beta signaling involves NOX4 in fibrotic responses and cellular transformations often intersecting with other proteins like Smad3. In the nitric oxide signaling pathway interactions with eNOS affect the bioavailability of nitric oxide impacting vascular function. These relationships indicate NOX4's role in managing oxidative stress and maintaining vascular homeostasis through specific signaling cascades involving these proteins.
Specifications
Form
Lyophilized
General info
Function
NADPH oxidase that catalyzes predominantly the reduction of oxygen to H2O2 (PubMed : 14966267, PubMed : 15356101, PubMed : 15927447, PubMed : 21343298, PubMed : 25062272). Can also catalyze to a smaller extent, the reduction of oxygen to superoxide (PubMed : 10869423, PubMed : 11032835, PubMed : 15155719, PubMed : 15572675, PubMed : 15927447, PubMed : 16019190, PubMed : 16179589, PubMed : 16230378, PubMed : 16324151, PubMed : 25062272). May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity (PubMed : 16019190). May regulate insulin signaling cascade (PubMed : 14966267). May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB (PubMed : 15356101, PubMed : 15572675). May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation (PubMed : 16324151). Promotes ferroptosis, reactive oxygen species production and reduced glutathione (GSH) levels by activating NLRP3 inflammasome activation and cytokine release (PubMed : 39909992).. Isoform 4. NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor (PubMed : 15721269, PubMed : 23393389). Involved in redox signaling in vascular cells (PubMed : 23393389). Modulates the nuclear activation of ERK1/2 and the ELK1 transcription factor, and is capable of inducing nuclear DNA damage (PubMed : 23393389).. Isoform 3. Lacks superoxide-generating NADPH oxidase activity.
Post-translational modifications
Deubiquitinated by USP19.. Isoform 4. N-glycosylated and glycosylation is required for its proper function.. Isoform 3. N-glycosylated.
Target data
Product promise
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