| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALAS1 |
| Uniprot No | P13196 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-98aa |
| 氨基酸序列 | MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALST AAVHYQQIKETPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLP |
| 预测分子量 | 36 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ALAS1重组蛋白的3篇参考文献示例(注：以下为虚构内容，仅作格式参考)：
1. **《重组ALAS1蛋白在大肠杆菌中的高效表达与酶活性分析》**
*作者：Zhang et al., 2020*
**摘要**：本研究成功构建了ALAS1的重组表达载体，利用大肠杆菌系统实现高效可溶性表达，并通过亲和层析纯化获得高纯度蛋白。酶动力学实验表明，重组ALAS1在体外催化效率接近天然酶，为血红素合成机制研究提供了工具。
2. **《ALAS1突变体重组蛋白的功能缺陷与遗传性卟啉症关联研究》**
*作者：Wang et al., 2018*
**摘要**：通过定点突变技术构建了ALAS1常见致病突变体(如R517H)，发现突变蛋白的稳定性及催化活性显著降低。该研究揭示了ALAS1功能异常导致卟啉症患者的血红素合成障碍分子机制。
3. **《线粒体靶向重组ALAS1在小鼠模型中的治疗潜力评估》**
*作者：Liu et al., 2021*
**摘要**：开发了一种融合线粒体定位序列的重组ALAS1蛋白，并在贫血模型小鼠中验证其疗效。结果显示，该蛋白可有效恢复肝脏血红素水平，为ALAS1缺陷相关疾病的蛋白替代疗法提供了依据。
**注**：实际文献需通过PubMed或Web of Science等平台以关键词“ALAS1 recombinant protein”检索真实发表论文。
**Background of ALAS1 Recombinant Protein**
5-Aminolevulinate synthase 1 (ALAS1) is a mitochondrial enzyme that catalyzes the first and rate-limiting step in heme biosynthesis: the condensation of glycine and succinyl-CoA to form 5-aminolevulinic acid (ALA). This reaction is essential for producing heme, a critical cofactor for hemoglobin, cytochromes, and other hemoproteins. ALAS1 is ubiquitously expressed in non-erythroid tissues, distinguishing it from ALAS2. the erythroid-specific isoform. Its activity is tightly regulated by cellular heme levels, iron availability, and oxidative stress, reflecting its role in maintaining metabolic homeostasis.
Recombinant ALAS1 protein is engineered using genetic engineering techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems to ensure proper folding and post-translational modifications. Purified ALAS1 retains enzymatic activity and is widely used in biochemical studies to investigate heme biosynthesis pathways, enzyme kinetics, and regulatory mechanisms. Researchers employ it to model diseases linked to ALAS1 dysfunction, such as porphyrias—a group of disorders caused by heme metabolism defects—and to explore conditions like iron-deficiency anemia or mitochondrial disorders.
Additionally, recombinant ALAS1 serves as a tool for drug discovery, enabling high-throughput screening of compounds that modulate enzyme activity. This is particularly relevant for developing therapies targeting ALAS1 overexpression, which is implicated in certain cancers or neurotoxic effects due to ALA accumulation. Structural studies using recombinant ALAS1 have also advanced understanding of substrate binding, catalytic mechanisms, and mutations causing hereditary defects.
In summary, ALAS1 recombinant protein is a vital resource for unraveling heme biology, disease mechanisms, and therapeutic interventions, bridging molecular insights with clinical applications.
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