For immunochemical detection of tryptophan hydroxylase
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Tryptophan Hydroxylase (Phospho-Ser58) Polyclonal Antibody

Item No. 10009397

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • TPH
Immunogen
phosphopeptide corresponding to amino acid residues surrounding phospho-Ser58 of TPH
Formulation (Request formulation change)
Peptide affinity-purified antibody
Host
Rabbit
Applications
WB
Species Reactivity
(+) Rabbit TPH(+) Bovine TPH (expected)(+) Canine TPH (expected)(+) Human TPH (expected)(+) Mouse TPH (expected)(+) Non-human primate TPH (expected)(+) Rat TPH (expected)(+) Xenopus TPH (expected)(+) Zebrafish TPH (expected)
Origin
Animal/Rabbit
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Tryptophan hydroxylase (TPH) catalyzes the 5-hydroxylation of tryptophan, which is the first step in the biosynthesis of indoleamines (serotonin and melatonin).1 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).2,3 Both PKA and CaM K II phosphorylate Ser58 which lies within the regulatory domain of TPH.4

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Martinez, A., Knappskog, P.M., and Haavik, J. A structural approach into human tryptophan hydroxylase and its implications for the regulation of serotonin biosyntheis. Curr. Med. Chem. 8(9), 1077-1091 (2001).

    2. Jiang, G.C., Yohrling, G.J., Schmitt, J.D., et al. Identification of substrate orienting and phosphorylation sites within typtophan hydroxylase using homology-based molecular modeling. J. Mol. Biol. 302, 1005-1017 (2000).

    3. Johansen, P.A., Jennings, I., Cotton, R.G., et al. Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A. J. Neurochem. 66, 817-823 (1996).

    4. Kuhn, D.M., Arthur, R., Jr., and States, J.C. Phosphorylation and activation of brain tryptophan hydroxylase: Identification of serine-58 as a substrate site for protein kinase A. J. Neurochem. 68, 2220-2223 (1997).