Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
DDC Antibody recognizes endogenous levels of total DDC protein.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val33 of human DDC protein. Antibodies are purified by protein A and peptide affinity chromatography.
L-DOPA decarboxylase (DDC) is a pyridoxal 5-phosphate (PLP)-dependent enzyme that catalyzes the decarboxylation of L-DOPA to dopamine (1) and L-5HTP to serotonin (2). By catalyzing the reaction to produce dopamine, DDC is involved in many important metabolic processes and plays a central role in the complex neuroendocrine-immune regulatory network (1). DDC is expressed in the central nervous system (3), but has also been detected in some peripheral organs such as the liver and adrenal gland, as well as leukocytes of rat and human (1). DDC is thought to be the sole enzyme responsible for the synthesis of the trace amines 2-phenylethylamine, p-tyramine, and tryptamine, which are considered to act as neuromodulators (2,4). DDC is also regarded as a general biomarker for neuroendocrine tumors (3).
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