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

The antibody has been directly tested for reactivity in Western blots with rat tissue. It is anticipated that the antibody will react with bovine, mouse and zebra fish based on the fact that these species have 100% homology with the amino acid sequence used as antigen.

Affinity Purified

100 uL in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per mL BSA and 50% glycerol.

Aliquot and store at -20°C or below. Avoid multiple freeze-thaw cycles.

Type:
Antigen: TPH2
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype:
Reactivity: Mouse, Rat, Bovine, Xenopus