|Predicted||Bovine, Mouse, Zebrafish|
|Calculated MW||55 KDa|
|Other Names||Tryptophan 5-hydroxylase 2, Neuronal tryptophan hydroxylase, Tryptophan 5-monooxygenase 2, Tph2, Ntph|
|Target/Specificity||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser19 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 ~55k tryptophan hydroxylase protein phosphorylated at Ser19.|
|Precautions||Phospho-Ser19 Tryptophan Hydroxylase 2 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). CaM K II phosphorylates Ser19 which lies within the regulatory domain of TPH2 (McKinney et al., 2005).
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.
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.
McKinney J, Knappskog PM, Haavik J (2005) Different properties of the central and peripheral forms of human tryptophan hydrpxylase. J Neurochem 92(2):311-20.
Kuhn DM, Sakowski SA, Geddes TJ, Wilkerson C, Haycock JW (2007) Phosphorylation and activation of tryptophan hydroxylase 2: identification of serine-19 as the substrate site for calcium, calmodulin-dependent protein kinase II. J Neurochem 103(4):1567-73.
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