Anti-SMOX Antibody Picoband® Fluoro647 Conjugated

Spermine oxidase is an enzyme that in humans is encoded by the SMOX gene. Polyamines are ubiquitous polycationic alkylamines which include spermine, spermidine, putrescine, and agmatine. These molecules participate in a broad range of cellular functions which include cell cycle modulation, scavenging reactive oxygen species, and the control of gene expression. These molecules also play important roles in neurotransmission through their regulation of cell-surface receptor activity, involvement in intracellular signalling pathways, and their putative roles as neurotransmitters. This gene encodes an FAD-containing enzyme that catalyzes the oxidation of spermine to spermadine and secondarily produces hydrogen peroxide. Multiple transcript variants encoding different isoenzymes have been identified for this gene, some of which have failed to demonstrate significant oxidase activity on natural polyamine substrates. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism.

Widely expressed. Isoform 1 and isoform 2 are expressed at higher level in brain and skeletal muscle. Isoform 7 is found in brain and spleen, isoform 10 is widely expressed but found at lower level in heart, kidney, liver and lung.

Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N1-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal.

1. Hartz, P. A. Personal Communication. Baltimore, Md. 6/20/2014. 2. Murray-Stewart, T., Wang, Y., Devereux, W., Casero, R. A., Jr. Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics. Biochem. J. 368: 673-677, 2002. 3. Pledgie, A., Huang, Y., Hacker, A., Zhang, Z., Woster, P. M., Davidson, N. E., Casero, R. A., Jr. Spermine oxidase SMO (PAOh1), not N (1) -acetylpolyamine oxidase PAO, is the primary source of cytotoxic H2O2 in polyamine analogue-treated human breast cancer cell lines. J. Biol. Chem. 280: 39843-39851, 2005.