Recombinant NOX4 protein (His tag)

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This recombinant protein product features a 157-amino acid fragment (residues 268-424) of human NADPH oxidase 4 (NOX4), encompassing the complete FAD-binding FR-type domain (residues 304-419). This fragment serves as an essential tool for investigating the catalytic mechanisms and functional roles of NOX4's FAD-binding domain in reactive oxygen species production and redox signaling pathways.

NADPH oxidase 4 (NOX4) is a membrane-bound enzyme primarily catalyzing the reduction of oxygen to hydrogen peroxide (H₂O₂), with minor superoxide production. It functions as an oxygen sensor regulating potassium channels and HIF1A activity, participates in insulin signaling, apoptosis, bone resorption, and NFKB activation. Recent evidence indicates NOX4 promotes ferroptosis through NLRP3 inflammasome activation and cytokine release. The full-length protein localizes to multiple cellular compartments including the cytoplasm, endoplasmic reticulum membrane, cell membrane, focal adhesions, and nucleus, reflecting its diverse regulatory roles. Isoform-specific functions include nuclear redox signaling (Isoform 4) and loss of oxidase activity (Isoform 3). The provided fragment targets the critical FAD-binding domain essential for NADPH oxidase function.

268-424