Anti-gp91phox (NOX2) Antibody

Cytochrome b-245 heavy chain (UniProt: P04839; also known as CGD91-phox, Cytochrome b(558) subunit beta, Cytochrome b558 subunit beta, Heme-binding membrane glycoprotein gp91phox, NADPH oxidase 2, Neutrophil cytochrome b 91 kDa polypeptide, Superoxide-generating NADPH oxidase heavy chain subunit, gp91-1, gp91-phox, p22 phagocyte B-cytochrome) is encoded by the CYBB (also known as NOX2) gene (Gene ID: 1536) in Human. Gp91phox is a multi-pass membrane glycoprotein of the NADPH oxidase family that contains three extracellular domains, six transmembrane domains, and four cytoplasmic domains. It contains four iron binding sites and has a ferric oxidoreductase domain that is localized in the amino acids 54-286. It is a critical component of the membrane-bound oxidase of phagocytes that generates superoxide and plays an important role in the host defense function of phagocytic cells. It also functions as a voltage-gated proton channel that mediates the H+ currents of resting phagocytes. It can undergo polyubiquitination at lysine 48 by RNF145 that triggers its endoplasmic reticulum-associated degradation. Clone 54.1 recognizes the conserved carboxy-terminal domain of NOX family proteins and shows higher specificity for NOX2 and reduced reactivity with NOX3, NOX4, and NOX1 in the descending order. Mutations in CYBB gene are known to cause granulomatous disease that is characterized by the inability of neutrophils and phagocytes to kill ingested leading to life-threatening bacterial and fungal infections. (Ref.: (Ref.: Burritt, JB., et al. (2003). J. Immunol. 170 (12); 6082-6089).