Phosphospecific Antibody

Tyrosine hydroxylase (TH) catalyzes the conversion of tyrosine to L-DOPA, which is the rate limiting step in the biosynthesis of catecholamines such as dopamine, adrenalin and noradrenalin. Nerve cells with TH content are referred to as catecholaminergic cells and occurs mainly in the brain and adrenal glands. Defects in TH are the cause of Segawa syndrome, translating in progressive difficulty in walking. The activity of TH is also regulated by phosphorylation.

Tyrosine hydroxylase (TH) catalyzes the conversion of tyrosine to L-DOPA, which is the rate limiting step in the biosynthesis of catecholamines such as dopamine, adrenalin and noradrenalin. Nerve cells with TH content are referred to as catecholaminergic cells and occurs mainly in the brain and adrenal glands. Defects in TH are the cause of Segawa syndrome, translating in progressive difficulty in walking. The activity of TH is also regulated by phosphorylation.

Tryptophan 5-hydroxylase 1 (TPH) catalyzes the following reaction: L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin. TPH belongs to the biopterin-dependent aromatic amino acid hydroxylase family. Both PKA and CaM K II phosphorylate Ser58 which lies within the regulatory domain of TPH.

Tau protein promotes microtubule assembly and stability. Tau is also involved in the establishment and maintenance of neural polarity. The C-terminus domain of Tau binds to axonal microtubules whereas the N-terminus domain binds to neural plasma membrane components, therefore suggesting that Tau protein functions as a linker between the two. Axonal polarity is predetermined by tau localization in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.