Phospho-p40phox (Thr154) Antibody detects endogenous levels of p40phox only when phosphorylated at threonine 154. This antibody does not cross-react with other phosphorylated phox subunits.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr154 of human p40phox. Antibodies are purified by protein A and peptide affinity chromatography.
Background
The phagocytic NADPH oxidase is a multiprotein enzyme that catalyzes the reduction of oxygen to superoxide in response to invasion of pathogens into the body. The NADPH oxidase consists of 6 subunits, the membrane-bound p91phox and p22phox heterodimer (also known as cytochrome b558), the cytoplasmic complex of p40phox, p47phox and p67phox, and the small GTPase Rac2. Activation of NADPH oxidase is initiated by phosphorylation of the cytosolic complex, which induces comformational changes of the complex and ultimately leads to the translocation of the cytoplasmic complex to the membrane to form an active enzyme with cytochrome b558 (1). Thr154 and Ser315 of p40 phox have been identified as PKC phosphorylation sites modified during activation of the phagocyte NADPH oxidase (2).