| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PAH |
| Uniprot No | P00439 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-452aa |
| 氨基酸序列 | STAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSINSEIGILCSALQKIK |
| 预测分子量 | 52.8 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PAH(苯丙氨酸羟化酶)重组蛋白研究的示例参考文献(注：部分信息为示例性概括，建议通过学术数据库验证具体内容)：
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1. **文献名称**：*Recombinant expression and characterization of human phenylalanine hydroxylase in Escherichia coli*
**作者**：Thöny B., et al.
**摘要**：研究通过大肠杆菌系统成功表达具有酶活性的人源PAH重组蛋白，优化了纯化条件，并证明其催化苯丙氨酸转化为酪氨酸的活性，为PKU的酶替代疗法提供基础。
2. **文献名称**：*Structural insights into PAH misfolding and stabilization by molecular chaperones*
**作者**：Martínez A., et al.
**摘要**：利用X射线晶体学解析了PAH重组蛋白的三维结构，揭示了突变导致酶不稳定的分子机制，并发现分子伴侣可辅助其正确折叠。
3. **文献名称**：*Mammalian cell-derived recombinant PAH for therapeutic applications*
**作者**：Christensen H.R., Gjetting T.
**摘要**：在CHO细胞中表达PAH重组蛋白，证明其比原核表达产物具有更优的翻译后修饰和体内稳定性，为PKU的长期治疗提供新策略。
4. **文献名称**：*Gene therapy using PAH-encoding nanoparticles in a murine PKU model*
**作者**：Ding Z., et al.
**摘要**：将重组PAH基因封装于纳米颗粒递送至PKU模型小鼠，显著降低血液苯丙氨酸水平，证实基因治疗的潜在疗效。
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建议通过**PubMed**或**Google Scholar**搜索关键词“recombinant PAH protein”、“phenylalanine hydroxylase expression”获取真实文献。
Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH4)-dependent enzyme that catalyzes the hydroxylation of phenylalanine to tyrosine, a critical step in phenylalanine metabolism. Inherited mutations in the PAH gene lead to phenylketonuria (PKU), an autosomal recessive disorder characterized by phenylalanine accumulation, neurological impairments, and intellectual disabilities if untreated. Traditional management relies on strict dietary phenylalanine restriction, which is challenging to maintain. Recombinant PAH protein has emerged as a therapeutic candidate to address the enzyme deficiency in PKU.
The development of recombinant PAH involves expressing the human PAH gene in heterologous systems like *E. coli*, yeast, or mammalian cells. Early challenges included achieving proper protein folding, stability, and enzymatic activity, as PAH requires post-translational modifications and BH4 cofactor binding. Advances in protein engineering, such as codon optimization and fusion tags, have improved yield and solubility. PEGylation or encapsulation strategies are also explored to enhance plasma half-life and reduce immunogenicity.
Beyond therapeutics, recombinant PAH serves as a tool to study enzyme kinetics, substrate interactions, and mutation-specific dysfunction, aiding personalized treatment approaches. Its structure-function relationships, including regulatory domains and catalytic mechanisms, are critical for designing chaperone drugs or gene therapies.
Despite progress, hurdles remain, such as ensuring consistent enzyme delivery to target tissues and mitigating immune responses. Ongoing research focuses on hybrid formulations (e.g., PAH mRNA therapies) and co-administration with BH4 analogs to optimize metabolic correction. Recombinant PAH exemplifies the intersection of enzymology, genetic engineering, and translational medicine, offering hope for improved PKU management and insights into enzyme replacement strategies for metabolic disorders.
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