The NOXA2 protein, also known as p67phox (phagocyte oxidase), is a critical regulatory component of the NADPH oxidase complex, a key enzyme system responsible for generating reactive oxygen species (ROS) in phagocytic cells. This multi-subunit complex plays a vital role in innate immunity by producing superoxide anions (O₂⁻) during the respiratory burst, a process essential for pathogen elimination. The p67phox protein contains multiple functional domains, including SH3 domains and a PB1 domain, which mediate interactions with other oxidase components like p47phox and the GTPase RAC1. Its activation is tightly regulated, involving phosphorylation and membrane translocation during complex assembly.
Mutations in the NCF2 gene encoding p67phox are linked to chronic granulomatous disease (CGD), a rare immunodeficiency disorder characterized by impaired microbial killing. Beyond immunity, p67phox contributes to redox signaling in non-phagocytic cells and has been implicated in inflammatory diseases, neurodegenerative conditions, and cancer progression.
Antibodies targeting p67phox/NOXA2 are widely used in research to study its expression, subcellular localization, and functional interactions. Common applications include Western blotting, immunofluorescence, and immunohistochemistry to assess protein levels in immune cells, characterize CGD mutations, or investigate ROS-related mechanisms in disease models. These antibodies often recognize conserved epitopes in human, mouse, or rat homologs, enabling cross-species comparative studies. Validation typically involves knockout cell lines or patient-derived samples with known mutations to confirm specificity.