Th (tyrosine hydroxylase) is a homotetramer that has regulatory, catalytic and tetramerization domains. The gene is located on chromosome llpl5.

The antibody detects endogenous levels of total Tyrosine Hydroxylase protein.

Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms . This enzyme is required for embryonic development since TH knockout mice die before or at birth . Levels of transcription, translation and posttranslational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31 and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH . Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels.

Peptide sequence around aa. 29-33 (V-T-S-P-R), according to the protein NP_954986.2

Th (tyrosine hydroxylase) plays an important role in catecholamine synthesis as it helps in the hydroxylation of L-tyrosine to l-DOPA (l-3,4-dihydroxyphenylalanine). Th gene mutation results in tyrosine hydroxylase deficiency.

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Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

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