Dopa Decarboxylase/DDC Antibody Summary
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Dopa Decarboxylase/DDC by Western Blot. Western blot of bovine adrenal medulla lysate showing specific immunolabeling of the ~55 kDa DDC protein.
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Background: Dopa Decarboxylase/DDC
DOPA decarboxylase (Aromatic-L-amino acid decarboxylase; also DDC) is a 54 kDa member of the alpha -family of pyroxidal phosphate enzymes. Functional DDC is a homodimeric, pyridoxal phosphate-dependent enzyme that calatyzes the decarboxylation of DOPA to dopamine, L-tryptophan to tryptamine, and 5-hydroxytryptophan to serotonin. Both dopamine and serotonin are important neurotransmitters. It also demonstrates deaminase activity, and is regulated by O2 availability. Bovine DDC is 487 amino acids (aa) in length and contains an N-terminal decarboxylase domain (aa 35-414) and a C-terminal pyroxidal binding site (L303). Bovine DDC is 88% and 86% aa identical to human and rat DDC, respectively.
- Kang, U.J. and T.H. Joh (1990) Brain Res. Mol. Brain Res. 8:83.
- Ichinose, H. et al. (1989) Biochem. Biophys. Res. Commun. 164:1024.
- Moore, P.S. et al. (1996) Biochem. J. 315:249.
- Bertoldi, M. and C.B. Voltattorni (2003) Biochim. Biophys. Acta 1647:42.
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