epitope corresponding to phosphorylated Thr 154 of p40-phox of human origin
recommended for detection of Threonine 154 phosphorylated p40-phox of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including canine and porcine
p40-phox Background Information Nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase is a multimeric enzyme system that mediates electron transport from NADPH in the cytoplasm to molecular oxygen in the phagosome, thereby generating reactive oxidant intermediates. Upon neutrophil stimulation, NADPH-oxidase and other cytosolic elements localize to the cell membrane from the cytosol to form a complex which produces phagocytic oxygen radicals. There are a number of cytosolic proteins that are involved in NADPH-oxidase activation/ deactivation, including p47-phox, p67-phox, p40-phox and the small GTP-binding protein, Rac. Activation of NADPH oxidase is accompanied by the phosphorylation of cytosolic components p40-phox, p47-phox and p67-phox. The PKC consensus phosphorylation sights Thr 154 and Ser 315 in p40-phox are phosphorylated during activation of NADPH oxidase. p40-phox can promote oxidase activation by increasing the affinity of p47-phox for NADPH-oxidase. However, p40-phox appears to down-regulate oxidase function as well, by competing with an SH3 domain interaction between other essential oxidase components.
