Analytical Data
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Gene name
TH
- Application
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Alternative Names
TH；TYH；Tyrosine 3-monooxygenase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P07101
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Expression Region
1-528aa
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AA Sequence
MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
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Molecular Weight
58.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of TH (tyrosine hydroxylase) recombinant proteins has gained significant attention due to their pivotal role in the biosynthesis of catecholamines, which are crucial neurotransmitters involved in various physiological processes, including mood regulation, stress response, and motor control. TH is the rate-limiting enzyme in the synthesis of dopamine, norepinephrine, and epinephrine, making it a key target for research related to neurological disorders such as Parkinson's disease, depression, and anxiety. Advances in biotechnology have enabled the production of TH recombinant proteins, allowing researchers to investigate their structure, function, and regulatory mechanisms in greater detail. These recombinant proteins can be utilized for functional assays, drug screening, and understanding the enzymatic pathways and genetic regulation involved in catecholamine synthesis. Additionally, studying TH in a recombinant form can unveil potential therapeutic targets and strategies for ameliorating catecholamine-related disorders. Given the increasing prevalence of these conditions in modern society, the exploration of TH recombinant proteins not only enhances our fundamental understanding of neurochemistry but also holds potential for the development of novel interventions and treatments.
