Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery

Product Highlight

Mouse anti-M13 phage coat protein g8p

Antibodies recognising M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface. The monoclonal antibodies manufactured and supplied by Exalpha react with either the pIII (g3p) or pVIII (g8p) proteins of M13 filamentous bacteriophage. All antibodies are available in a purified format. The antibodies are fully validated and are suitable for a wide range of techniques including:

  • ELISA
  • Flow Cytometry
  • Western Blot
  • Immunohistochemistry
  • Immunoprecipitation
For more information, click here for our M13 Bacteriophage information page.

News

Two more of our excellent products have been published by PubMed:

Potential actionable targets in appendiceal cancer detected by immunohistochemistry, fluorescent in situ hybridization, and mutational analysis
Borazanci, E., et al., J. Gastrointest. Oncol., 8, 164-172 (2017)
Using Exalpha SPARC Antibody (Cat. No. X1867P)

Molecular mechanism underlying the pharmacological interactions of the protein kinase C-β inhibitor enzastaurin and erlotinib in non-small cell lung cancer cells
Steen, N.V., et al., Am. J. Cancer Res., 7, 816-830 (2017)
Using Exalpha's FITC labeled anti PY20 Antibody (Cat. No. X1017)

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

Host/Source

Mouse

Clone

T101

Isotype

IgG1

Product Type

Monoclonal Antibody

Reactivity

Human, Mouse, Porcine (most mammalian species)

Applications

Immunohistochemistry, Immunofluorescense, Enzyme Immunoassay

Purification

Provided as whole ascites

Size

100 µl

Price (USD)

$361

Background

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.

Immunogen

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.

Formulation

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:

SwissProtP52895Human

References

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 (±)-trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene in fortified rat liver subcellular fractions. Carcinogenesis, 13: 1575-1582, 1992.

4. Flowers-Geary, L., Harvey, R. G., and Penning, T. M. Cytotoxicity of polycyclic aromatic hydrocarbon o-quinones in rat and human hepatoma cells. Chem. Res. Toxicol., 6: 252-260, 1993.

5. Shen, H., Kauvar, L., and Tew, K. D. Importance of glutathione and associated enzymes in drug response. Oncol. Res., 9: 295-302, 1997.

6. Ax, W., Soldan, M., Koch, L., and Maser, E. Development of daunorubicin resistance in tumour cells by induction of carbonyl reduction. Biochem. Pharmacol., 59: 293-300, 2000.