| 纯度 | > 85 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALAD |
| Uniprot No | P13716 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-330aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMQPQSV LHSGYFHPLL RAWQTATTTL NASNLIYPIF VTDVPDDIQP ITSLPGVARY GVKRLEEMLR PLVEEGLRCV LIFGVPSRVP KDERGSAADS EESPAIEAIH LLRKTFPNLL VACDVCLCPY TSHGHCGLLS ENGAFRAEES RQRLAEVALA YAKAGCQVVA PSDMMDGRVE AIKEALMAHG LGNRVSVMSY SAKFASCFYG PFRDAAKSSP AFGDRRCYQL PPGARGLALR AVDRDVREGA DMLMVKPGMP YLDIVREVKD KHPDLPLAVY HVSGEFAMLW HGAQAGAFDL KAAVLEAMTA FRRAGADIII TYYTPQLLQW LKEE |
| 预测分子量 | 39 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ALAD(δ-氨基乙酰丙酸脱水酶)重组蛋白研究的3篇代表性文献摘要概括：
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1. **文献名称**: "Cloning, Expression, and Characterization of Recombinant Human δ-Aminolevulinate Dehydratase"
**作者**: Jaffe EK, Ali S, Mitchell LW
**摘要**: 该研究报道了人源ALAD基因在大肠杆菌中的重组表达与纯化，分析了重组酶的动力学特性及锌离子对其活性的调控作用，为研究遗传性ALAD缺乏症(ADP)的分子机制提供了模型。
2. **文献名称**: "Structural Insights into ALAD Mutants Linked to Porphyria by Recombinant Protein Analysis"
**作者**: Breinig S, Kervio E, Schmitt G
**摘要**: 通过重组表达多种ALAD突变体蛋白，结合X射线晶体学解析突变对酶三维结构的影响，揭示了特定氨基酸残基突变导致酶活性丧失的分子基础，为卟啉症治疗策略提供理论支持。
3. **文献名称**: "Heterologous Production of ALAD in Yeast for Heavy Metal Biosensing Applications"
**作者**: Wang Y, Li C, Zhang R
**摘要**: 研究在酿酒酵母中高效表达重组ALAD蛋白，并开发基于该酶铅离子抑制效应的生物传感器，证明其在环境重金属污染检测中的潜在应用价值。
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**备注**：以上文献信息为基于领域知识的模拟概括，实际文献需通过PubMed、Web of Science等平台检索关键词"ALAD recombinant protein"或结合具体研究方向筛选。如需具体文献，建议补充研究场景或时间范围以进一步筛选。
**Background of ALAD Recombinant Protein**
Delta-aminolevulinic acid dehydratase (ALAD), also known as porphobilinogen synthase, is a key enzyme in the heme biosynthesis pathway. It catalyzes the condensation of two molecules of δ-aminolevulinic acid (ALA) to form porphobilinogen (PBG), a critical step in tetrapyrrole production. ALAD is a metalloenzyme requiring zinc ions for activity and is ubiquitously expressed in prokaryotes and eukaryotes. In humans, ALAD dysfunction is linked to metabolic disorders such as ALAD deficiency porphyria, a rare genetic condition characterized by neurovisceral symptoms, and susceptibility to lead poisoning, as lead inhibits ALAD activity by displacing zinc.
Recombinant ALAD protein is produced using biotechnological platforms like *E. coli* or yeast expression systems, enabling large-scale, high-purity production for research and therapeutic applications. Its recombinant form retains enzymatic activity and structural integrity, making it invaluable for studying heme biosynthesis mechanisms, enzyme kinetics, and metal ion interactions. Additionally, recombinant ALAD serves as a tool for developing diagnostics for porphyrias or lead exposure and as a potential therapeutic agent in enzyme replacement strategies.
Recent studies also explore ALAD’s role beyond heme synthesis, including its interaction with cellular redox systems and possible implications in neurodegenerative diseases. The engineered protein’s stability and modifiable properties further support drug discovery and industrial biotechnology applications. Overall, ALAD recombinant protein bridges basic biochemical research and clinical innovation, offering insights into metabolic diseases and environmental toxicity.
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