CBR3 Antibody

Carbonyl Reductase-3 (CBR3) is an enzyme that plays a crucial role in the reduction of carbonyl compounds to their corresponding alcohols. This enzyme is part of the short-chain dehydrogenase/reductase (SDR) family, which includes a variety of enzymes with NAD(P)H-dependent oxidoreductase activity .

The CBR3 gene is located on chromosome 21 in humans and consists of three exons spanning approximately 11.2 kilobases . The gene is closely linked to another carbonyl reductase gene, CBR1, and both genes exhibit high homology in their amino acid sequences . The CBR3 protein is classified as a monomeric NADPH-dependent oxidoreductase .

CBR3 catalyzes the reduction of a wide range of biologically and pharmacologically active carbonyl compounds, including steroids, prostaglandins, and various xenobiotics . The enzyme has been shown to have low NADPH-dependent oxidoreductase activity and acts on several orthoquinones, as well as non-quinone compounds such as isatin and the anticancer drug oracin . The best substrate for CBR3 is 1,2-naphthoquinone, suggesting a role in protecting against the cytotoxicity of exogenous quinones .

CBR3 is ubiquitously expressed in various tissues, although its expression levels are generally lower compared to CBR1 . Immunofluorescence staining has revealed that CBR3 proteins are localized in the cytosol of cells .

Mouse anti-human CBR3 antibodies are commonly used in research to study the expression and function of the CBR3 enzyme. These antibodies are generated by immunizing mice with human CBR3 protein, leading to the production of antibodies that specifically recognize and bind to human CBR3. These antibodies can be used in various applications, including Western blotting, immunohistochemistry, and enzyme-linked immunosorbent assays (ELISA).

The study of CBR3 and its related pathways has significant implications for understanding various physiological and pathological processes. For instance, CBR3’s role in reducing carbonyl compounds is crucial for detoxifying reactive carbonyl species, which can cause cellular damage. Additionally, the enzyme’s activity towards anticancer drugs like oracin highlights its potential relevance in cancer therapy .