Anti-Catalase Antibody Picoband® (Dylight594 Conjugate)

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. .

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.

Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat<br> Immunohistochemistry (Paraffin-embedded Section), 0.5-1μg/ml, Human, Mouse, Rat, By Heat<br> Immunohistochemistry (Frozen Section), 0.5-1μg/ml, Human<br> Immunocytochemistry/Immunofluorescence, 2μg/ml, Human<br> Flow Cytometry (Fixed), 1-3μg/1x10⁶ cells, Human