Analytical Data
-
基因名
TH
- Application
-
别名
TH；TYH；Tyrosine 3-monooxygenase
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P07101
-
表达区间
1-528aa
-
氨基酸序列
MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
-
分子量
58.6 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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
Recombinant Mouse Arid5a Protein，His
Cat：PA2000-3825
Recombinant Human FABP12 Protein，His
Cat：PA1000-1071
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.
