| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GCH1 |
| Uniprot No | P30793 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-250aa |
| 氨基酸序列 | MEKGPVRAPA EKPRGARCSN GFPERDPPRP GPSRPAEKPP RPEAKSAQPA DGWKGERPRS EEDNELNLPN LAAAYSSILS SLGENPQRQG LLKTPWRAAS AMQFFTKGYQ ETISDVLNDA IFDEDHDEMV IVKDIDMFSM CEHHLVPFVG KVHIGYLPNK QVLGLSKLAR IVEIYSRRLQ VQERLTKQIA VAITEALRPA GVGVVVEATH MCMVMRGVQK MNSKTVTSTM LGVFREDPKT REEFLTLIRS |
| 预测分子量 | 27,9 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GCH1重组蛋白的模拟参考文献示例，基于常见研究方向构建：
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1. **文献名称**: "Expression and Purification of Recombinant Human GTP Cyclohydrolase 1 (GCH1) in *E. coli*"
**作者**: Smith J, et al.
**摘要**: 本研究报道了利用大肠杆菌表达系统高效表达人源GCH1重组蛋白，并通过亲和层析成功纯化。酶活性分析表明，重组蛋白具有催化BH4前体合成的功能，为体外研究GCH1酶动力学提供了基础。
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2. **文献名称**: "Functional Characterization of Recombinant GCH1 Mutants in Parkinsonian Models"
**作者**: Lee S, et al.
**摘要**: 通过哺乳动物细胞表达系统制备了多种GCH1突变体重组蛋白，发现特定突变(如R198W)显著降低酶活性，导致多巴胺合成障碍。该研究为遗传性运动障碍的分子机制提供了实验依据。
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3. **文献名称**: "Crystal Structure of GTP Cyclohydrolase 1 Reveals Novel Insights into BH4 Biosynthesis"
**作者**: Zhang H, et al.
**摘要**: 首次解析了重组人GCH1蛋白的X射线晶体结构(分辨率2.1Å)，揭示了底物结合口袋的关键氨基酸残基，并阐明了其多聚化机制，为靶向GCH1的药物设计奠定结构基础。
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4. **文献名称**: "Recombinant GCH1 Delivery Ameliorates Hypertension in Rat Models"
**作者**: Gupta R, et al.
**摘要**: 通过腺病毒载体递送重组GCH1至高血压模型大鼠，显著提升血管内皮BH4水平，改善一氧化氮依赖性血管舒张功能，证明GCH1蛋白治疗的潜在临床应用价值。
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**注**：以上为模拟示例，实际文献需通过PubMed、Google Scholar等平台检索关键词(如"recombinant GCH1"、"GTPCH1 expression")。建议结合具体研究方向筛选近年高引论文。
GCH1 (GTP cyclohydrolase 1) is a rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin (BH4), an essential cofactor for neurotransmitters (e.g., dopamine, serotonin) and nitric oxide synthases. It catalyzes the conversion of GTP to dihydroneopterin triphosphate, the first and critical step in BH4 production. Dysregulation of GCH1 is linked to neurological disorders, including dopa-responsive dystonia, and cardiovascular diseases due to impaired nitric oxide signaling.
Recombinant GCH1 protein is engineered using expression systems like E. coli or mammalian cells to produce purified, functional enzyme for research and therapeutic applications. Its production enables detailed studies of BH4 metabolism, enzyme kinetics, and molecular interactions. Researchers use it to model pathogenic mutations, screen potential drugs, or develop enzyme replacement therapies. Structural analysis of recombinant GCH1 (often via X-ray crystallography) has revealed insights into its catalytic mechanism and regulatory domains, aiding targeted drug design.
In biotechnology, recombinant GCH1 supports large-scale BH4 synthesis, which is costly to produce chemically. It also serves as a tool for diagnosing genetic deficiencies by comparing activity levels in clinical samples. Recent studies explore its role in immune modulation and cancer, as BH4 influences T-cell function and tumor microenvironment dynamics.
Despite progress, challenges remain in stabilizing the protein for long-term storage and optimizing delivery methods for therapeutic use. Ongoing research focuses on fusion tags to enhance solubility and gene therapy approaches to address GCH1 deficiencies at the genetic level.
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