Catalase
Catalase (CAT) is a heme-containing antioxidant enzyme that breaks down hydrogen peroxide into water and oxygen. It sits in the peroxisome of nearly all aerobic cells and forms a key part of the defence against oxidative stress. Browse Assay Genie's current range of Catalase research reagents below, or read on for the biology behind the target.
Catalase catalyses the degradation of hydrogen peroxide (H2O2) generated by peroxisomal oxidases, converting it to water and oxygen. This protects cells from the toxic effects of hydrogen peroxide, a reactive oxygen species. Catalase is a heme enzyme and is present in the peroxisome of nearly all aerobic cells, where it is localised to the peroxisome matrix. UniProt also reports that catalase promotes the growth of several cell types, including T-cells, B-cells, myeloid leukaemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblasts.
The human CAT gene encodes catalase and belongs to the catalase family, with the enzyme assigned EC 1.11.1.6. Orthologous genes are named Cat in both mouse and rat, which makes rodent models a practical route for studying its biology. The gene is catalogued under HGNC:1516, NCBI Gene 847 and UniProt P04040.
Oxidative stress is hypothesised to contribute to many chronic or late-onset diseases, including diabetes, asthma, Alzheimer's disease, systemic lupus erythematosus, rheumatoid arthritis and cancers. Because catalase removes hydrogen peroxide, it is often studied in this context. Polymorphisms in the gene have been associated with decreased catalase activity. To date, acatalasemia is the only disease known to be caused by this gene.
Catalase is a key antioxidant enzyme that mitigates the toxic effects of hydrogen peroxide, making it a central readout of cellular defence against oxidative stress.
Catalase degrades hydrogen peroxide produced by peroxisomal oxidases and resides in the peroxisome matrix, so it is widely used to study peroxisomal function.
Oxidative stress is hypothesised to play a role in diabetes, asthma, Alzheimer's disease, lupus, rheumatoid arthritis and cancers, all areas where catalase is studied.
UniProt reports that catalase promotes growth of T-cells, B-cells, melanoma cells and fibroblasts, linking the enzyme to proliferation studies.
Catalase degrades hydrogen peroxide, produced by peroxisomal oxidases, into water and oxygen. This protects cells from peroxide toxicity. It is a heme enzyme found in the peroxisome of nearly all aerobic cells, and it is a key antioxidant in the defence against oxidative stress.
Acatalasemia is the only disease known to be caused by the CAT gene. Polymorphisms have been associated with reduced catalase activity. Oxidative stress, which catalase helps to limit, is hypothesised to contribute to diabetes, asthma, Alzheimer's disease, lupus, rheumatoid arthritis and cancers.
Yes. The human gene CAT has orthologues named Cat in mouse and rat. The enzyme is present in the peroxisome of nearly all aerobic cells. For cross-species work, check the datasheet of any product for its validated reactivity.
Other enzymes with research reagents at Assay Genie, including the cathepsin protease family.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P04040; product specifications from Assay Genie datasheets.