Antigen: human NAD+-dependent 15-hydroxy prostaglandin dehydrogenase (15-hydroxy PGDH) amino acids 92-105 (AGVNNEKNWEKTLQ) · Host: rabbit · Application(s): WB; other applications not tested · NAD+-dependent 15-hydroxy PGDH catalyzes the oxidation of prostaglandins to 15-keto metabolites, which have greatly reduced biological activity.1 Human NAD+-dependent 15-hydroxy PGDH is a 266 amino acid protein with a molecular weight of 29 kDa and is expressed in multiple tissues including lung, placenta, and kidney.2 The enzyme belongs to a large family of short-chain alcohol dehydrogenases, which exhibit amino acid identity ranging from 15-30%.3,4 An NADP+-dependent 15-hydroxy PGDH, which is also part of this enzyme family, exhibits only 20% amino acid identity to the NAD+-dependent enzyme.5 The peptide used as the antigen for preparation of the 15-hydroxy PGDH antibody is highly conserved across several species (see above), but has only minor homology to other proteins within the short-chain alcohol dehydrogenase family of enzymes (only the alanine and glycine at the N-terminus of the sequence appear to be conserved).3 |
1 Hansen, H.S. 15-Hydroxyprostaglandin dehydrogenase. A review. Prostaglandins 12 647-679 (1976). 2 Ensor, C.M., Yang, J., Okita, R.T., et al. Cloning and sequence analysis of the cDNA for human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. J Biol Chem 265 14888-14891 (1990). 3 J?rnvall, H., Persson, B., Krook, M., et al. Short-chain dehydrogenases/reductases (SDR). Biochemistry 34 6003-6013 (1995). 4 Krook, M., Marekov, L., J?rnvall, H. Purification and structural characterization of placental NAD+-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family. Biochemistry 29 738-743 (1990). 5 Wermuth, B. NADP-dependent 15-hydroxyprostaglandin dehydrogenase is homologous to NAD-dependent 15-hydroxyprostaglandin dehydrogenase and other short-chain alcohol dehydrogenases. Prostaglandins 44 5-9 (1992). |