| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TH |
| Uniprot No | P07101 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-528aa |
| 氨基酸序列 | MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG |
| 预测分子量 | 58,6 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇与TH(酪rosine羟化酶)重组蛋白相关的文献摘要示例：
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1. **文献名称**：*Expression and Purification of Recombinant Human Tyrosine Hydroxylase in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：本研究描述了一种利用大肠杆菌表达系统高效表达人源酪氨酸羟化酶(TH)的方法，并通过亲和层析纯化获得高活性重组蛋白，为酶学研究和药物开发提供基础。
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2. **文献名称**：*Structural Characterization of Recombinant Rat Tyrosine Hydroxylase Using X-ray Crystallography*
**作者**：Lee B, et al.
**摘要**：通过X射线晶体学解析了大鼠重组TH蛋白的三维结构，揭示了其催化域的关键氨基酸残基和四氢生物蝶呤(BH4)辅因子的结合位点，为设计TH活性调节剂提供结构依据。
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3. **文献名称**：*Functional Analysis of Recombinant TH in a Parkinson’s Disease Cell Model*
**作者**：Chen L, et al.
**摘要**：利用昆虫细胞表达系统制备重组TH蛋白，并在帕金森病细胞模型中验证其恢复多巴胺合成的功能，证明其在基因治疗中的潜在应用价值。
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(注：以上文献为示例性内容，实际引用时需核实真实存在的论文信息。)
**Background of TH Recombinant Protein**
Tyrosine hydroxylase (TH) is a rate-limiting enzyme responsible for catalyzing the conversion of the amino acid tyrosine to L-3.4-dihydroxyphenylalanine (L-DOPA), a critical step in the biosynthesis of catecholamines, including dopamine, norepinephrine, and epinephrine. These neurotransmitters and hormones play essential roles in regulating mood, motor control, stress responses, and cardiovascular functions. Dysregulation of TH activity is linked to neurological disorders such as Parkinson’s disease, where dopamine deficiency occurs, and psychiatric conditions like depression.
TH recombinant protein is produced via genetic engineering, typically by expressing the *TH* gene in bacterial (e.g., *E. coli*), yeast, or mammalian cell systems. This approach enables large-scale production of purified, bioactive TH protein with consistent quality, overcoming limitations of isolating the enzyme from native tissues. Recombinant TH retains catalytic activity and structural features, making it valuable for *in vitro* studies, including enzyme kinetics, inhibitor screening, and structural analysis.
Research applications of TH recombinant protein span drug discovery (e.g., identifying TH modulators for Parkinson’s), studying pathogenic mutations, and developing enzyme replacement strategies. Additionally, it serves as a tool for generating catecholamines in cell-based models or bioreactors. Recent advances in protein engineering have focused on enhancing TH stability, solubility, or activity through site-directed mutagenesis or fusion tags. Challenges remain in optimizing expression systems for humanized post-translational modifications and ensuring functional consistency across batches.
Overall, TH recombinant protein is a pivotal resource for advancing both basic neuroscience and therapeutic innovations targeting catecholamine-related diseases.
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