| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | phhA |
| Uniprot No | P30967 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-297aa |
| 氨基酸序列 | MNDRADFVVPDITTRKNVGLSHDANDFTLPQPLDRYSAEDHATWATLYQRQCKLLPGRACDEFMEGLERLEVDADRVPDFNKLNQKLMAATGWKIVAVPGLIPDDVFFEHLANRRFPVTWWLREPHQLDYLQEPDVFHDLFGHVPLLINPVFADYLEAYGKGGVKAKALGALPMLARLYWYTVEFGLINTPAGMRIYGAGILSSKSESIYCLDSASPNRVGFDLMRIMNTRYRIDTFQKTYFVIDSFKQLFDATAPDFAPLYLQLADAQPWGAGDVAPDDLVLNAGDRQGWADTEDV |
| 预测分子量 | 35.1 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phhA重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Expression and characterization of recombinant human phenylalanine hydroxylase in E. coli: Effect of N-terminal modifications"*
**作者**：Thöny, B., et al.
**摘要**：研究通过在大肠杆菌中表达人源phhA基因(PAH)，优化重组蛋白的可溶性表达，并分析N端修饰对酶活性和稳定性的影响，为苯丙酮尿症治疗提供参考。
2. **文献名称**：*"Crystal structure of the phenylalanine hydroxylase from Pseudomonas aeruginosa: Insights into substrate specificity"*
**作者**：Kobe, B., et al.
**摘要**：解析铜绿假单胞菌phhA重组蛋白的晶体结构，揭示其底物结合域的关键氨基酸残基，阐明其催化苯丙氨酸羟基化为酪氨酸的分子机制。
3. **文献名称**：*"Heterologous expression of phhA in Pichia pastoris for L-tyrosine production"*
**作者**：Wang, Q., et al.
**摘要**：将来自嗜热菌的phhA基因在毕赤酵母中高效表达，优化发酵条件后显著提升L-酪氨酸产量，为工业级芳香族氨基酸生产提供新策略。
注：以上文献为示例性质，实际引用需根据具体研究方向补充真实发表的论文信息。
**Background of phhA Recombinant Protein**
The *phhA* gene, originally identified in *Pseudomonas* species, encodes a phenol hydroxylase enzyme critical for the microbial degradation of aromatic compounds, particularly phenol and its derivatives. This enzyme catalyzes the first step in the catabolic pathway, converting phenol into catechol via monooxygenation, which is subsequently metabolized through the *meta*-cleavage pathway. The *phhA* system plays a vital role in environmental bioremediation, enabling bacteria to utilize phenolic pollutants as carbon and energy sources.
Recombinant phhA protein is produced by cloning the *phhA* gene into expression vectors (e.g., *E. coli*), followed by induction and purification. This approach overcomes limitations of low native expression in wild-type strains and allows scalable production. The recombinant protein is often engineered with affinity tags (e.g., His-tag) to facilitate purification via chromatography. Structural and functional studies of phhA have revealed insights into its substrate specificity, cofactor requirements (e.g., NADPH), and regulatory mechanisms, such as its dependence on the transcriptional activator PhhR.
Research on phhA recombinant protein has applications in biodegradation technologies, biosensor development for phenol detection, and enzymatic synthesis of catechol derivatives. Additionally, it serves as a model system for studying oxygenase enzyme mechanics and microbial adaptation to toxic environments. Challenges include optimizing enzyme stability and activity under industrial conditions, which are areas of ongoing biotechnological innovation.
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