Tryptofaan (fosfo Ser58) Hydroxylase Antilichaam

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.

24848

P09810

P09810

Human, Mouse, Rat

TPH (Ser58) polyclonal antibody was raised against a synthetic phosphopeptide corresponding to amino acid residues surrounding the phosphoSer58 of TPH.

Unconjugated

Primary Antibodies

Neuroscience, Phospho-Specific

Affinity Purified

Batch dependent

Phospho-Specific

Blue Ice

For long term storage –80˚ C is recommended, but shorter term storage at –20˚ C is also acceptable as aliquots may be taken without freeze/thawing due to the presence of 50% glycerol. Stable for one year.

55

Tryptophan Hydroxylase antibody is specific immunolabeling of the ~55k TPH protein phosphorylated at Ser58 in Western blots of human dorsal Raphe nucleus.

Applications include Dot Blots (DB) and Western Blots (WB) . When internally tested under ideal conditions the working dilutions were 1:1000 for DB and WB.

Tph1

Tryptophan hydroxylase 1

Rattus norvegicus

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

Jiang, 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 molecular modeling, " J. Mol. Biol., 302 (2000) 1005 - 1017.

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) 26219-26225.

Kuhn, 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. Neurochem. 68 (1997) 2220 - 2223.

WB

136122

Liquid