TPH1 (phospho-S260) polyclonal antibody

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) .

Western blot (WB) analysis of p-TPH1 (S260) pAb at 1:500 dilution Lane1:HEK293T whole cell lysate (40µg) Lane2:The Lung tissue lysate of Mouse (40µg) Lane3:LO2 whole cell lysate (40µg) Lane4:C6 whole cell lysate (40µg)