| 纯度 | >90%SDS-PAGE. |
| 种属 | rat |
| 靶点 | a1M |
| Uniprot No | Q63041 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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. |
以下是关于重组α1-微球蛋白(a1M)的3篇代表性文献示例(注：文献信息为模拟概括，建议通过学术数据库核实具体内容)：
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1. **文献名称**：*Recombinant α1-microglobulin protects against ischemia-reperfusion injury in a mouse kidney model*
**作者**：Smith J, et al.
**摘要**：研究重组a1M在小鼠肾脏缺血再灌注损伤中的保护作用，证实其通过抑制氧化应激和炎症反应减轻肾小管损伤，提示其在急性肾损伤治疗中的潜力。
2. **文献名称**：*Structural and functional characterization of recombinant human α1-microglobulin variants*
**作者**：Zhang L, et al.
**摘要**：通过基因工程构建不同突变体重组a1M，分析其抗氧化活性与结构稳定性的关系，发现C34位点对维持蛋白功能关键，为优化治疗性a1M设计提供依据。
3. **文献名称**：*A novel bacterial expression system for high-yield production of bioactive α1-microglobulin*
**作者**：Andersson B, et al.
**摘要**：开发基于大肠杆菌的重组a1M高效表达纯化工艺，通过密码子优化和折叠辅助策略实现可溶性蛋白高产，为大规模临床应用奠定基础。
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**提示**：建议在PubMed或Web of Science中以“recombinant alpha-1-microglobulin”为关键词检索最新研究，重点关注其在抗氧化、肾脏疾病及炎症相关疾病中的应用机制。
**Background of α1M Recombinant Protein**
α1-Macroglobulin (α1M) is a large, evolutionarily conserved glycoprotein belonging to the protease inhibitor superfamily. It is primarily synthesized in the liver and circulates in body fluids, including blood and cerebrospinal fluid. Native α1M acts as a broad-spectrum protease inhibitor, neutralizing a wide range of proteolytic enzymes through a unique "bait-and-trap" mechanism. Upon protease interaction, α1M undergoes conformational changes, entrapping the enzyme and signaling for its clearance via receptor-mediated endocytosis (e.g., LRP1). Beyond protease regulation, α1M exhibits anti-inflammatory, antioxidant, and cytoprotective properties, including binding and detoxifying heme and reactive oxygen species (ROS).
Recombinant α1M (rα1M) is produced using biotechnological platforms (e.g., mammalian or bacterial expression systems) to overcome limitations of plasma-derived α1M, such as low yield and pathogen risks. The recombinant form retains the functional domains of native α1M, including the thiol ester bond critical for protease entrapment and the receptor-binding region. Studies highlight its therapeutic potential in conditions involving proteolytic imbalance or oxidative stress, such as preeclampsia, neurodegenerative diseases, and acute kidney injury. For instance, rα1M mitigates placental inflammation in preeclampsia models and reduces neural damage in stroke by scavenging toxic metabolites.
Current research focuses on optimizing production, enhancing stability, and exploring targeted delivery systems. Its dual role as a protease inhibitor and molecular chaperone positions rα1M as a promising multifunctional biologic for treating complex pathologies linked to inflammation and tissue damage.
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