DDH is a member of aldo-keto reductase superfamily1,2, which catalyzes reduction of aldehyde or ketone to a corresponding alcohol by using NADH or NADPH as a cofactor. In liver, the enzyme is abundantly located in the cytoplasm as a monomeric 34-36 kDa protein3,4. Interestingly, by differential display Shen et al.5 has shown that overexpression of DDH could be identified in ethacrynic acid-induced drug-resistant human colon cancer cells. Detection of DDH overexpression in drug-resistant human stomach cancer cells, which were selected by the gradual adaptation to daunorubicin, further suggested that DDH might be associated with the drug-resistance in cancer cells6. In a recent study, DDH expression was further shown to have prognostic significance in patients with NSCLC. By using an immunohistochemical method to determine DDH expression in surgical specimens, DDH expression was identified in patients with leukemia, lung cancer, esophageal cancer, transitional cancer and breast cancer. Furthermore, overexpression of DDH was confirmed by immunoblotting and in situ hybridization. Correlation between clinicopathological parameters and DDH expression as well as the prognostic significance of DDH expression in patients with advanced cancer was indicated.

Hybridoma produced by the fusion of splenocytes from mice immunized with recombinant type 2 dihydrodiol dehydrogenase from human lung cancer and mouse myeloma cells.

Human breast cancer and porcine liver tissue; Recognizes the DD1 and DD2 isoforms.

Provided as solution in phosphate buffered saline with 0.08% sodium azide

Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles

Left: Immunoperoxidase staining of formalin-fixed paraffin embedded human lung cancer tissue showing cytoplasmic localization of dihydrodiol dehydrogenase. Right: Western blot analysis using DDH antibody (Cat. No. X1265M) on porcine liver (A) and breast cancer (B).