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.
200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml.
SDS-PAGE Analysis of Purified TPH1 Mouse Monoclonal Antibody (TPH1/7662). Confirmation of Purity and Integrity of Antibody.
Formalin-fixed, paraffin-embedded human kidney cancer stained with TPH1 Mouse Monoclonal Antibody (TPH1/7662). HIER: Tris/EDTA, pH9.0, 45min. 2°C: HRP-polymer, 30min. DAB, 5min.
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