| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HPDL |
| Uniprot No | Q96IR7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-371aa |
| 氨基酸序列 | MAAPALRLCHIAFHVPAGQPLARNLQRLFGFQPLASREVDGWRQLALRSGDAVFLVNEGAGSGEPLYGLDPRHAVPSATNLCFDVADAGAATRELAALGCSVPVPPVRVRDAQGAATYAVVSSPAGILSLTLLERAGYRGPFLPGFRPVSSAPGPGWVSRVDHLTLACTPGSSPTLLRWFHDCLGFCHLPLSPGEDPELGLEMTAGFGLGGLRLTALQAQPGSIVPTLVLAESLPGATTRQDQVEQFLARHKGPGLQHVGLYTPNIVEATEGVATAGGQFLAPPGAYYQQPGKERQIRAAGHEPHLLARQGILLDGDKGKFLLQVFTKSLFTEDTFFLELIQRQGATGFGQGNIRALWQSVQEQSARSQEA |
| 预测分子量 | 46.8 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HPDL重组蛋白的参考文献示例(注：以下为虚构示例，实际文献需通过学术数据库查询)：
1. **文献名称**: "Cloning and Biochemical Characterization of Human HPDL Recombinant Protein"
**作者**: Wiessemer, J. et al.
**摘要**: 研究报道了HPDL基因的克隆、重组蛋白在大肠杆菌中的表达及纯化方法，分析了其酶活性与底物特异性，揭示了HPDL在酪氨酸代谢中的潜在作用。
2. **文献名称**: "Structural Insights into HPDL Mutations Associated with Neurological Disorders"
**作者**: Smith, R.L. & Chao, H.
**摘要**: 通过X射线晶体学解析了重组HPDL蛋白的三维结构，探讨了致病突变对其催化功能的影响，为神经退行性疾病的机制研究提供依据。
3. **文献名称**: "HPDL Deficiency: Functional Rescue by Recombinant Protein in Cellular Models"
**作者**: Johnson, M. et al.
**摘要**: 利用重组HPDL蛋白在患者来源的细胞模型中恢复酶活性，验证了其治疗HPDL相关神经发育障碍的潜力，并评估了蛋白稳定性与递送策略。
4. **文献名称**: "High-Throughput Screening of HPDL Inhibitors Using Recombinant Enzyme Assays"
**作者**: Lee, S. et al.
**摘要**: 开发了基于重组HPDL蛋白的高通量筛选平台，用于发现新型小分子抑制剂，为代谢性疾病药物研发提供工具。
**建议**：如需真实文献，可通过PubMed或Google Scholar搜索关键词“HPDL recombinant protein”“HPDL gene function”或结合疾病关键词(如“neurodegeneration”)筛选近期研究。
**Background of HPDL Recombinant Protein**
The HPDL (4-hydroxyphenylpyruvate dioxygenase-like) protein is a less-characterized member of the dioxygenase family, encoded by the *HPDL* gene in humans. Initially identified through homology to 4-hydroxyphenylpyruvate dioxygenase (HPD), a key enzyme in tyrosine catabolism, HPDL shares structural similarities but exhibits distinct functional roles. While HPD catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisate in the tyrosine degradation pathway, HPDL’s precise enzymatic activity remains unclear, though it is hypothesized to participate in redox or metabolic processes, potentially involving metal ion coordination (e.g., iron or magnesium).
Interest in HPDL surged following genetic studies linking *HPDL* mutations to severe neurological disorders, including early-onset mitochondrial encephalopathy, spastic paraplegia, and Leigh-like syndromes. These findings suggest HPDL is critical for neuronal function, possibly through maintaining mitochondrial homeostasis or regulating oxidative stress. However, mechanistic insights remain limited, necessitating further biochemical characterization.
Recombinant HPDL protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), enables functional and structural studies. Its production involves cloning the *HPDL* gene into expression vectors, optimizing conditions for solubility and yield, and purifying the protein using affinity chromatography. Recombinant HPDL facilitates investigations into substrate specificity, enzyme kinetics, and interactions with potential cofactors or binding partners.
Current research focuses on elucidating HPDL’s role in cellular metabolism and disease pathogenesis, with therapeutic implications for mitochondrial disorders. Additionally, recombinant HPDL serves as a tool for drug screening or antibody development. Despite progress, unresolved questions about its physiological substrates and regulatory mechanisms highlight the need for continued interdisciplinary exploration.
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