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 the first and rate-limiting step in the biosynthesis of serotonin in the central nervous system and melatonin in the pineal gland.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB:1:500~1:1000 IHC:1:50~1:200
Application Notes:
TPH1 (Phospho-S58) polyclonal antibody detects endogenous levels of TPH1 protein only when phosphorylated at Ser58.
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