| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HPD |
| Uniprot No | P32754 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-393aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMTTYSDKGAKPERGRFLHFHSVTFWVGNAK QAASFYCSKMGFEPLAYRGLETGSREVVSHVIKQGKIVFVLSSALNPWNK EMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAKIMREPWVEQDKFGK VKFAVLQTYGDTTHTLVEKMNYIGQFLPGYEAPAFMDPLLPKLPKCSLEM IDHIVGNQPDQEMVSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVA NYEESIKMPINEPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRH LRERGLEFLSVPSTYYKQLREKLKTAKIKVKENIDALEELKILVDYDEKG YLLQIFTKPVQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQNLRGN LTNMETNGVVPGM |
| 预测分子量 | 47 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3篇关于HPD重组蛋白的模拟参考文献(内容为虚构，仅作示例)：
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1. **文献名称**: *Expression and Characterization of Recombinant Human HPD for Tyrosinemia Therapy*
**作者**: Smith J, et al.
**摘要**: 研究通过大肠杆菌系统重组表达人源HPD蛋白，优化纯化工艺并验证其酶活性。结果表明，重组HPD可降解酪氨酸代谢毒性产物，为酪氨酸血症Ⅰ型的酶替代疗法提供潜在方案。
2. **文献名称**: *Crystal Structure Analysis of Recombinant HPD from Pseudomonas putida*
**作者**: Lee H, Zhang R.
**摘要**: 解析了恶臭假单胞菌来源的HPD重组蛋白晶体结构，揭示其底物结合域的关键氨基酸残基，为设计高效HPD突变体以提升工业生物催化效率奠定基础。
3. **文献名称**: *Heterologous Production of HPD in Yeast for Metabolic Engineering Applications*
**作者**: García M, et al.
**摘要**: 在毕赤酵母中异源表达HPD重组蛋白，成功增强菌株对芳香族化合物的降解能力，证明其在合成生物学和环境污染修复中的潜在应用价值。
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(注：以上文献信息为模拟生成，实际研究需通过学术数据库检索确认。)
**Background of HPD Recombinant Protein**
HPD (4-hydroxyphenylpyruvate dioxygenase) is a key enzyme involved in the tyrosine degradation pathway, catalyzing the conversion of 4-hydroxyphenylpyruvate (HPP) to homogentisate. This reaction is critical in the metabolism of aromatic amino acids and is linked to several metabolic disorders, such as type III tyrosinemia, where HPD deficiency leads to the accumulation of toxic intermediates.
Recombinant HPD protein is produced using genetic engineering techniques, typically by inserting the HPD gene into expression systems like *E. coli*, yeast, or mammalian cells. This allows large-scale production of the enzyme for research and therapeutic applications. The recombinant form retains the enzymatic activity and structural features of the native protein, enabling studies on its mechanism, substrate specificity, and interaction with inhibitors.
HPD has garnered attention in drug development, particularly for treating hereditary tyrosinemia and metabolic diseases. Inhibitors targeting HPD, such as nitisinone, are used clinically to block tyrosine breakdown, alleviating symptoms in patients. Additionally, recombinant HPD serves as a tool for high-throughput screening of novel therapeutics or enzyme replacement strategies.
Beyond medicine, HPD’s role in plant and microbial metabolism has implications for agriculture and biotechnology. For example, engineering HPD activity in crops could influence stress resistance or secondary metabolite production.
Overall, recombinant HPD protein bridges fundamental research and applied sciences, offering insights into metabolic pathways and enabling innovations in healthcare and biotechnology. Its study continues to reveal new therapeutic targets and biotechnological applications.
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