Anti-PIPOX Antibody Picoband® Fluoro647 Conjugated

PIPOX (Pipecolic Acid And Sarcosine Oxidase, also known as L-pipecolate oxidase) is a Protein Coding gene. The PIPOX gene, located on 17q11.2, is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, rat, chicken, zebrafish, C.elegans, S.pombe, N.crassa, A.thaliana, rice, and frog. This enzyme oxidizes L-pipecolic acid with the concomitant production of H2O2 in the peroxisome of the normal human liver. Pipecolate, an intermediate of the lysine catabolic pathway, is oxidized to Δ1 -piperideine-6-carboxylate (P6C) by the PIPOX. Diseases associated with PIPOX include Inflammatory Bowel Disease 15 and Zellweger Syndrome. Among its related pathways are Lysine degradation and Viral mRNA Translation. 215 organisms have orthologs with the human gene PIPOX.

1. Dodt, G., Kim, D., Reimann, S., McCabe, K., Gould, S. J., Mihalik, S. J. The human L-pipecolic acid oxidase is similar to bacterial monomeric sarcosine oxidases rather than D-amino acid oxidases. Cell Biochem. Biophys. 32: 313-316, 2000. 2. Dodt, G., Kim, D. G., Reimann, S. A., Reuber, B. E., McCabe, K., Gould, S. J., Mihalik, S. J. L-pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases. Biochem. J. 345: 487-494, 2000. 3. IJlst, L., de Kromme, I., Oostheim, W., Wanders, R. J. A. Molecular cloning and expression of human L-pipecolate oxidase. Biochem. Biophys. Res. Commun. 270: 1101-1105, 2000.