Anti-Catalase Antibody Picoband® Fluoro488 Conjugated

Catalase is a key antioxidant enzyme in the bodies defensing against oxidative stress. It is also a heme enzyme that is present in the peroxisome of nearly all aerobic cells. Catalase converts the reactive oxygen species hydrogen peroxide to water and oxygen and thereby mitigates the toxic effects of hydrogen peroxide. Oxidative stress is hypothesized to play a role in the development of many chronic or late-onset diseases such as diabetes, asthma, Alzheimer's disease, systemic lupus erythematosus, rheumatoid arthritis, and cancers. Polymorphisms in this gene have been associated with decreases in catalase activity but, to date, acatalasemia is the only disease known to be caused by this gene.

E. coli-derived human Catalase recombinant protein (Position: E344-L527) . Human Catalase shares 85.3% and 82.6% amino acid (aa) sequence identity with mouse and rat Catalase, respectively.

Expressed in the temporal lobe, frontal lobe, parietal lobe, hippocampus, and cerebellum. Also found in kidney, lung, liver, heart, skeletal muscle, placenta. .

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. .

1. Junien, C., Turleau, C., de Grouchy, J., Said, R., Rethore, M.-O., Tenconi, R., Dufier, J. L. Regional assignment of catalase (CAT) gene to band 11p13: association with the aniridia-Wilms' tumor-gonadoblastoma (WAGR) complex. Ann. Genet. 23: 165-168, 1980. 2. Ogata, M., Wang, D.-H., Ogino, K. Mammalian acatalasemia: the perspectives of bioinformatics and genetic toxicology. Acta Med. Okayama 62: 345-361, 2008. Note: Erratum: Acta Med. Okayama 63: 121-122, 2009. 3. Quan, F., Korneluk, R. G., Tropak, M. B., Gravel, R. A. Isolation and characterization of the human catalase gene. Nucleic Acids Res. 14: 5321-5335, 1986.