纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | TPH1 |
Uniprot No | P17752 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 105-420aa |
氨基酸序列 | MHHHHHHVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKY FADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNL PLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAF RVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLAS LGASEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSG HAKVKPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTIKRPF GVKYNPYTRSIQILKDTKSITSA |
预测分子量 | 37 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. |
以下是关于TPH1重组蛋白的3篇参考文献及其摘要概括:
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1. **文献名称**: *"Expression, purification, and kinetic characterization of recombinant human tryptophan hydroxylase-1"*
**作者**: McKinney J, Teigen K, Frøystein NA, et al.
**摘要**: 该研究报道了在大肠杆菌系统中成功表达并纯化重组人源TPH1蛋白,通过酶动力学分析揭示了其催化色氨酸转化为5-羟色胺前体的机制,并探讨了磷酸化对酶活性的调控作用。
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2. **文献名称**: *"Crystal structure of human tryptophan hydroxylase 1 in complex with serotonin and tetrahydrobiopterin"*
**作者**: Wang L, Erlandsen H, Fitzpatrick PF.
**摘要**: 研究通过X射线晶体学解析了重组人源TPH1与底物5-羟色胺及辅因子四氢生物蝶呤(BH4)的复合结构,阐明了底物结合位点和催化活性中心的分子机制,为靶向TPH1的药物设计提供结构基础。
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3. **文献名称**: *"Functional characterization of recombinant tryptophan hydroxylase-1 (TPH1) variants associated with psychiatric disorders"*
**作者**: Cichon S, Winge I, Mattheisen M, et al.
**摘要**: 该研究利用哺乳动物细胞表达系统制备多种TPH1突变体重组蛋白,发现特定突变导致酶活性和稳定性下降,提示TPH1功能异常可能与情绪障碍及精神疾病的发生相关。
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以上文献涵盖了TPH1重组蛋白的表达纯化、结构解析及功能研究,可为相关科研提供参考。如需具体文献链接或补充更多研究,可进一步说明。
**Background of TPH1 Recombinant Protein**
Tryptophan hydroxylase 1 (TPH1) is a rate-limiting enzyme that catalyzes the conversion of L-tryptophan to 5-hydroxytryptophan (5-HTP), the initial and critical step in serotonin biosynthesis. Serotonin, a key neurotransmitter and signaling molecule, regulates diverse physiological processes, including mood, digestion, and vascular function. TPH1 is primarily expressed in peripheral tissues, such as the enterochromaffin cells of the gut, pineal gland, and peripheral neurons, distinguishing it from TPH2. its isoform found in the central nervous system.
Recombinant TPH1 protein is produced through genetic engineering, typically by inserting the human *TPH1* gene into expression systems like *E. coli*, yeast, or mammalian cells (e.g., HEK293 or CHO cells). This allows large-scale production of purified, biologically active TPH1 for research and therapeutic applications. The recombinant form retains enzymatic activity, enabling studies on serotonin regulation, enzyme kinetics, and inhibitor screening.
TPH1 dysregulation is linked to multiple diseases, including gastrointestinal disorders, depression, and carcinoid tumors. Recombinant TPH1 serves as a vital tool for developing inhibitors targeting serotonin overproduction in conditions like irritable bowel syndrome or neuroendocrine tumors. It also aids in structural studies to map catalytic domains and post-translational modifications influencing enzyme activity.
Additionally, TPH1 recombinant protein is used to generate antibodies for diagnostic assays, enhancing detection of serotonin-related pathologies. Its role in peripheral serotonin synthesis has spurred interest in metabolic and immune modulation, positioning TPH1 as a potential therapeutic target for obesity, inflammation, and cardiovascular diseases.
In summary, recombinant TPH1 bridges basic research and clinical applications, offering insights into serotonin biology and pathways for drug discovery. Its study continues to uncover novel mechanisms in health and disease.
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