|Predicted||Bovine, Chicken, Human, Mouse, Monkey, Rat, Xenopus, Zebrafish|
|Calculated MW||55 KDa|
|Other Names||Tryptophan 5-hydroxylase 1, Tryptophan 5-monooxygenase 1, Tph1, Tph|
|Target/Specificity||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser58 conjugated to KLH.|
|Format||Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.|
|Antibody Specificity||Specific for the ~53k tryptophan hydroxylase protein phosphorylated at Ser58.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-Ser58 Tryptophan Hydroxylase 1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
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) Both PKA and CaM K II phosphorylate Ser58 which lies within the regulatory domain of TPH (Kuhn et al., 1997).
Jiang GC, Yohrling GJ, Schmitt JD, Vrana KE (2000) Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based molecular modeling. J Mol Biol 302:1005-1017.
Johansen PA, Jennings I, Cotton RG, Kuhn DM (1996) Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A. J Neurochem 66:817-823.
Kuhn, DM, Arthur, Jr, R, States, JC (1997) Phosphorylation and activation of brain tryptophan hydroxylase: identification of serine-58 as a substrate site for protein kinase A. J Neurochem 68:2220-2223.
Martinez A, Knappskog PM, Haavik J (2001) Structural approach into human tryptophan hydroxylase and its implications for the regulation of serotonin biosynthesis. Curr Med Chem 8:1077-1091.
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