OMA1-04051 detects tyrosine hydroxylase (TH) from all mamalian and some non-mamalian tissues.
OMA1-04051 has been successfully used in Western blot and immunohistochemical (frozen sections) procedures. By Western blot, this antibody detects a single ~60 kDa protein representing tyrosine hydroxylase from rat brain. In Western blots of recombinant human TH splice variants hTH1, hTH2, and hTH4, OMA1-04051 detects single bands spanning 60-65 kDa. Immunohistochemical staining of TH in human brain with OMA1-04051 results in strong labeling of dopaminergic neurons in the substantia nigra of human brain, which is consistent with high TH enzymatic activity in these neurons.
OMA1-04051 antigen is purified rat pheochromocytoma tyrosine hydroxylase.
Figure 1 shows Western blot detection of the ~ 60 kDa Tyrosine Hydroxylase protein from 10 ug of rat caudate lysate using OMA1-04051. |
Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamine neurotransmitters (dopamine, epinephrine, and norepinephrine). It is responsible for the conversion of L-tyrosine to L-dopa in the catecholamine synthesis pathway. In all species, catecholamine synthesis is regulated by the interaction of TH with a cofactor, tetrahydrobiopterin (BH4). BH4 binds to the TH catalytic domain, resulting in enzymatic activity. Unlike TH in non-primate species, four human TH mRNA splice variants (hTH1-hTH4) have been isolated. These variants are identical in their catalytic domain, but differ in their N-terminal, regulatory domains. Little information has been uncovered regarding the regulatory role of these isoforms in vivo.
The role of TH in the synthesis of catecholamine neurotransmitters suggests a correlation between the enzyme and a number of neuropathogenic diseases characterized by irregular catecholamine levels. Catecholamine level irregularities have been uncovered in Parkinson's disease, schizophrenia, and dystonia, as well as a variety of cardiovascular diseases. |
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