Anti-Duox2 Antibody Picoband® Fluoro647 Conjugated

Dual oxidase 2, also known as DUOX2 or ThOX2 (for thyroid oxidase), is an enzyme that in humans is encoded by the DUOX2 gene. The protein encoded by this gene is a glycoprotein and a member of the NADPH oxidase family. The synthesis of thyroid hormone is catalyzed by a protein complex located at the apical membrane of thyroid follicular cells. This complex contains an iodide transporter, thyroperoxidase, and a peroxide generating system that includes this encoded protein and DUOX1. This protein is known as dual oxidase because it has both a peroxidase homology domain and a gp91phox domain.

Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175) ; binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV) .

1. Caillou, B., Dupuy, C., Lacroix, L., Nocera, M., Talbot, M., Ohayon, R., Deme, D., Bidart, J.-M., Schlumberger, M., Virion, A. Expression of reduced nicotinamide adenine dinucleotide phosphate oxidase (ThoX, LNOX, Duox) genes and proteins in human thyroid tissues. J. Clin. Endocr. Metab. 86: 3351-3358, 2001. 2. De Deken, X., Wang, D., Many, M.-C., Costagliola, S., Libert, F., Vassart, G., Dumont, J. E., Miot, F. Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J. Biol. Chem. 275: 23227-23233, 2000. 3. Dupuy, C., Ohayon, R., Valent, A., Noel-Hudson, M.-S., Deme, D., Virion, A. Purification of a novel flavoprotein involved in the thyroid NADPH oxidase: cloning of the porcine and human cDNAs. J. Biol. Chem. 274: 37265-37269, 1999.