Anti-Tyrosine Hydroxylase Antibody

Recognizes an epitope outside of the regulatory N-terminus. Recognizes a protein of approximately 59-61 kDa by Western blot. Does not react with the following on Western Blots: purified dopamine-beta-hydroxylase, phenylalanine hydroxylase, trytophan hydroxylase, dehydropteridine reductase, sepiapterin reductase or phenethanolamine-N-methyl transferase (PNMT). Identifies a single ~60 kDa band on Western Blots of HeLa cells transfected to express human tyrosine hydroxylase.

Tyrosine Hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamine neurotransmitters dopamine, epinephrine, and norepinephrine and is responsible for converting L-tyrosine to L-dopa. Synthesis of catecholamines is regulated by the interaction of TH with its cofactor, tetrahydrobiopterin (BH4), and the substrates L-tyrosine and molecular oxygen. In humans, four TH mRNA splice variants (hTH1-hTH4) have been isolated, while subprimate species rely on a single form of TH. It is known that the hTH1-hTH4 variants are identical in their catalytic domain but differ in their N-terminal regulatory domains. Importantly, LNC1 reacts with the catalytic domain of TH and thus with all four isoforms of human TH. The role of TH in the synthesis of catecholamine neurotransmitters suggests a connection between the enzyme and a number of neuropathogenic diseases characterized by irregular catecholamine levels, such as Parkinson's disease, schizophrenia, and dystonia, as well as a variety of cardiovascular diseases.