Tryptophan Hydroxylase, phosphorylated (Ser58) (TPH, TPRH, MGC119994, Tryptophan 5-hydroxylase 1, Tryptophan 5-monooxygenase, Tryptophan 5-monooxygenase 1, Tryptophan Hydroxylase 1, TPH 1, TPH1)

Tryptophan hydroxylase (TPH) catalyzes the 5-hydroxylation of tryptophan, which is the first step in the biosynthesis of indoleamines (serotonin and melatonin). 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). Both PKA and CAM K II phosphorylate Ser58 which lies within the regulatory domain of TPH.\n\nApplications: \nSuitable for use in Western Blot and Dot Blot. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile glycerol (40-50%), aliquot and store at -20 degrees C. Aliquots are stable for at least 3 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

T9014-82C

Size

100ul

Applications

WB

Hosts

Rabbit

Reactivities

Hum

Form

As reported

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

References

Banik, U., Wang, G.A., Wagner, P.D. and Kaufman, S. \"Interaction of phosphorylated tryptophan hydroxylase with 14-3-3 proteins,\" J. Biol. Chem. 272 (1997) 26,219 - 26,225.\nJiang, G.C., Yohrling, G.J., Schmitt, J.D. and Vrana, K.E. \"Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based\nmolecular modeling,\" J. Mol. Biol. 302 (2000) 1005 - 1017.\nJohansen, P.A., Jennings, I., Cotton, R.G. and Kuhn, D.M. \"Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A,\" J. Neurochem. 66 (1996) 817 -\n823.\nJohansen, P.A., Jennings, I., Cotton, R.G. and Kuhn, D.M. \n\"Tryptophan hydroxylase is phosphorylated by protein kinase A,\" J. Neurochem. 65 (1995) 882 - 888.\nKuhn, D.M., Arthur, Jr., R. and States, J.C. \"Phosphorylation and activation of brain tryptophan hydroxylase: identification of serine-58 as a substrate site for protein kinase A,\" J.\nNeurochem. 68 (1997) 2220 - 2223.

Additional Info

Specific for the ~55kDa TPH protein phosphorylated at Ser58. Species Crossreactivity: Human.