protein

Tyrosine Hydroxylase Protein, Human (sf9, His)

HY-P73564

50 μg

620 USD

Tyrosine Hydroxylase Protein, Human (sf9, His)

proteins

Sf9 insect cells

50 μg

620 USD

Tyrosine hydroxylase is a key enzyme in the biosynthesis of catecholamines, catalyzing the conversion of L-tyrosine into L-dopa, which is the rate-limiting step in the synthesis of dopamine, norepinephrine, and epinephrine. Tyrosine is hydroxylated using tetrahydrobiopterin and oxygen. Tyrosine Hydroxylase Protein, Human (sf9, His) is the recombinant human-derived Tyrosine Hydroxylase protein, expressed by Sf9 insect cells , with N-His labeled tag. The total length of Tyrosine Hydroxylase Protein, Human (sf9, His) is 496 a.a., with molecular weight of ~57.6 kDa.

Human

Tyrosine Hydroxylase, a pivotal enzyme in the biosynthesis of catecholamines, facilitates the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), representing the rate-limiting step in the synthesis of neurotransmitters such as dopamine, noradrenaline, and adrenaline. Utilizing tetrahydrobiopterin and molecular oxygen, the enzyme orchestrates the hydroxylation of tyrosine to form L-Dopa, a critical precursor in catecholamine biosynthesis. While tyrosine is its primary substrate, the enzyme exhibits a broader substrate range, catalyzing the hydroxylation of phenylalanine and tryptophan with lower specificity. Moreover, Tyrosine Hydroxylase contributes to the positive regulation of the regression of retinal hyaloid vessels during postnatal development. Despite its central role in catecholamine synthesis, it is worth noting that the discussed instance of Tyrosine Hydroxylase lacks catalytic activity.

DYT14; TH; TYH dystonia 14; TYH; Tyrosine 3-monooxygenase

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 500 mM NaCl, pH 8.0, 10% Glycerol. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Room temperature in continental US; may vary elsewhere.