Exalpha Biologicals, Inc.

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FIX&PERM Cell Fixation and Permeabilization Kit

Flow cytometric analyses with monoclonal antibodies were so far mainly restricted to cell surface molecules. Intracellular structures such as cytoplasmic or nuclear enzymes, oncoproteins, cytokines, immunoglobulins etc. were largely excluded from such studies. Also excluded from flow cytometric studies were cytoplasmic localizations of well-established membrane molecules like CD3 and CD22, which, in their cytoplasmic form, are the most reliable lineage markers in undifferentiated leukemia. With the FIX&PERM® Kit flow cytometric analysis of intracellular antigens has become as easy as surface antigen studies. The only prerequisite is the availability of suitable antibody conjugates. Most of the available monoclonal antibody conjugates can be used with the FIX&PERM® Kit, some determinants are sensitive, however, to the fixation step involved. This and the optimal fixation time have to be tested for each reagent.


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We are pleased to announce that Peter Rutten has now started in his role as Operations Director here at Exalpha Biologicals Inc. Peter has a Master’s of Science degree in Industrial and Organizational Psychology and this has lead him down a very business orientated career path. Peter is looking forward to working with the team at Exalpha. Peters primary focus is the customer experience and he will be working with the Laboratory team, the Quality Control team and the Order Processing team to ensure this focus is achieved. We all wish Peter well in his new role.

Exalpha Biologicals, Inc.

Dihydrodiol Dehydrogenase

  • Product Code: X1265M
  • Size: 100 µl
  • Availability: In Stock In Stock
  • Price (USD): $361

Cat #

X1265M		 Quantity:      

Data Sheet

Product Name

Dihydrodiol Dehydrogenase







Product Type

Monoclonal Antibody


Human, Mouse, Porcine (most mammalian species)


Immunohistochemistry, Immunofluorescense, Enzyme Immunoassay


Provided as whole ascites


100 µl

Price (USD)



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.

Positive Control

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


Provided as solution in phosphate buffered saline with 0.02% sodium azide

Customer Storage

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

Product Image

Image Legend

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).

Database Links:



1. Vogel, K., Bentley, P., Platt, K. L., and Oesch, F. Rat liver cytoplasmic dihydrodiol dehydrogenase. J. Biol. Chem., 255: 9621-9625, 1980.

2. Cheng, K. C. Molecular cloning of rat liver 3 a-hydroxysteroid dehydrogenase and related enzymes from rat liver, kidney and lung. J. Steroid Biochem. Mol. Biol., 43: 1083-1088, 1992.

3. Shou, M., Harvey, R. G., and Penning, T. M. Contribution of dihydrodiol dehydrogenase to the metabolism of (