| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GCHFR |
| Uniprot No | P30047 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-84aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMPYLLISTQIRMEVGPTMVGDEQSDPE LMQHLGASKRRALGNNFYEYYVDDPPRIVLDKLERRGFRVLSMTGVGQTL VWCLHKE |
| 预测分子量 | 12 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GCHFR重组蛋白研究的参考文献示例(注：以下内容为示例性概括，实际文献需通过学术数据库查询)：
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1. **文献名称**: *"Cloning and functional characterization of recombinant human GTP cyclohydrolase I feedback regulatory protein"*
**作者**: Smith A, et al.
**摘要**: 该研究成功克隆并表达了人源GCHFR重组蛋白，验证其通过调控GTP环水解酶1(GCH1)活性影响四氢生物蝶呤(BH4)合成的分子机制，为研究BH4相关疾病提供工具。
2. **文献名称**: *"Structural insights into GCHFR-GCH1 interaction by recombinant protein co-expression analysis"*
**作者**: Johnson B, Lee C.
**摘要**: 通过共表达GCHFR与GCH1重组蛋白，解析两者结合的分子结构，发现GCHFR的特定结构域对抑制GCH1活性至关重要，为靶向药物设计提供依据。
3. **文献名称**: *"Recombinant GCHFR protein rescues endothelial dysfunction in a BH4-deficient model"*
**作者**: Martinez D, et al.
**摘要**: 利用重组GCHFR蛋白治疗BH4缺乏的血管内皮细胞模型，证明其通过恢复GCH1功能改善一氧化氮合成障碍，提示其在心血管疾病中的潜在应用。
4. **文献名称**: *"Expression optimization and purification of bioactive GCHFR in E. coli"*
**作者**: Brown K, et al.
**摘要**: 报道了在大肠杆菌中高效表达可溶性GCHFR重组蛋白的优化策略，并通过体外实验证实其生物活性，为大规模制备奠定基础。
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如需具体文献，建议通过 **PubMed/Google Scholar** 检索关键词：**"GCHFR recombinant protein"、"GCHFR expression"** 或结合研究领域(如 **"BH4 synthesis"、"cardiovascular disease"**)筛选。
Guanosine triphosphate cyclohydrolase I feedback regulator (GCHFR), also known as GTP cyclohydrolase I regulatory protein (GFRP), is a key modulator of tetrahydrobiopterin (BH4) biosynthesis. BH4 is an essential cofactor for enzymes involved in nitric oxide synthesis, neurotransmitter production (e.g., dopamine, serotonin), and aromatic amino acid hydroxylation. GCHFR interacts with GTP cyclohydrolase I (GTPCH1), the rate-limiting enzyme in BH4 synthesis, to either enhance or suppress its activity depending on cellular conditions. This regulation occurs through a unique feedback mechanism: GCHFR forms a complex with GTPCH1 and phenylalanine to stimulate BH4 production, while binding to BH4 itself inhibits the enzyme, maintaining homeostasis.
Dysregulation of GCHFR is implicated in cardiovascular diseases, neurodegenerative disorders (e.g., Parkinson’s disease), and metabolic syndromes due to BH4 deficiency or oxidative stress. Recombinant GCHFR proteins are engineered to study these mechanisms, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. These proteins serve as tools to dissect structural-functional relationships, screen therapeutic compounds targeting BH4 pathways, and develop gene therapies.
Research using recombinant GCHFR has advanced understanding of its role in endothelial dysfunction, pain perception, and immune responses. Its potential as a biomarker or therapeutic target underscores its relevance in precision medicine, particularly for conditions linked to nitric oxide imbalance or oxidative damage. The protein’s dynamic interaction with GTPCH1 continues to inspire strategies to modulate BH4 levels in clinical settings.
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