PAO-1 Antibody / Polyamine oxidase 1 / SMOX

Western blot: 0.5-1ug/ml,Immunohistochemistry (FFPE): 2-5ug/ml,Immunofluorescence: 5ug/ml,Flow cytometry: 1-3ug/million cells,Direct ELISA: 0.1-0.5ug/ml

Lyophilized from 1X PBS with 2% Trehalose

Spermine oxidase, also called Polyamine oxidase 1 (PAO-1), 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.

Antigen affinity purified

0.5mg/ml if reconstituted with 0.2ml sterile DI water

E. coli-derived recombinant human protein (amino acids E45-Q454) was used as the immunogen for the PAO-1 antibody.

Cytoplasmic, nuclear

Antigen affinity purified

Q9NWM0