Tryptophan Hydroxylase (Ser260) Antibody

Tryptophan hydroxylase (TPH) catalyzes the 5-hydroxylation of tryptophan, which is the first step in the biosynthesis of indoleamines (serotonin and melatonin) (Martinez et al., 2001) . In mammals, serotonin biosynthesis occurs predominantly in neurons which originate in the Raphe nuclei of the brain, and melatonin synthesis takes place within the pineal gland. Although TPH catalyzes the same reaction within the Raphe nuclei and the pineal gland, TPH activity is rate-limiting for serotonin but not melatonin biosynthesis. Serotonin functions mainly as a neurotransmitter, whereas melatonin is the principal hormone secreted by the pineal gland. The activity of TPH is enhanced by phosphorylation by cAMP-dependent protein kinase (PKA) and Ca2+/calmodulin kinase II (CaM K II) (Jiang et al., 2000; Johansen et al., 1996) . CaM K II phosphorylates Ser-260 which lies within the regulatory domain of TPH (Jiang et al., 2000) .

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Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser260 of rat tryptophan hydroxylase (TPH), conjugated to keyhole limpet hemocyanin (KLH) .

Specific for endogenous levels of the ~55 kDa tryptophan hydroxylase protein phosphorylated at Ser260. Immunolabeling is blocked by preadsorption with the phosphopeptide used as antigen, but not by the corresponding non-phosphopeptide.