Anti-Tryptophan Hydroxylase / TPH1, clone TPH1/7662

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Phenylalanine hydroxylase (PAH), tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH) comprise a small family of monooxygenases that use tetrahydropterine as a cofactor during the catabolism of aromatic L-amino acids. PAH, TH and TPH all contain catalytic domains with an amino-terminal regulatory domain and a short carboxy-terminal tetramerization domain. Each of these enzymes also contains a single ferrous iron atom, which is bound to two histidines and a glutamate, and is likely to be involved in the formation of the hydroxylating intermediate. TPH is both the first and rate-limiting-step in the biosynthesis of serotonin in the central nervous system and melatonin in the pineal gland. Alteration of TPH function may be a key factor in the pathology of several neuropsychiatric disorders associated with serotonin, including depression, aggression, alcoholism and schizophrenia. For instance, LDOPA, which is used as a common therapy for Parkinson s disease (PD) patients, inhibits TPH function which, subsequently, is thought to contribute to the onset of depression in PD patients. Protein function: Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate- determining step of serotonin biosynthesis. [The UniProt Consortium]