Tyrosine Hydroxylase Protein, Human (sf9, His)

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.

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.

Human

Sf9 insect cells

N-His

P07101-3 (P2-G497)

7054  [NCBI]

Partial

PTPDATTPQAKGFRRAVSELDAKQAEAIMSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG

Approximately 55-66 kDa, based on SDS-PAGE under reducing conditions.

≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of 20 mM Tris, 500 mM NaCl, pH 8.0, 10% Glycerol, 5% trehalose, 5% mannitol and 0.01% Tween 80.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.