| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Mb |
| Uniprot No | P02144 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-154aa |
| 氨基酸序列 | MGLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGATVLTALGGILKKKGHHEAEIKPLAQSHATKHKIPVKYLEFISECIIQVLQSKHPGDFGADAQGAMNKALELFRKDMASNYKELGFQG |
| 预测分子量 | 17,1 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Mb(肌红蛋白)重组蛋白的3篇模拟参考文献示例(内容为虚构，仅作格式参考)：
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1. **文献名称**: *Heterologous Expression and Purification of Recombinant Myoglobin in E. coli*
**作者**: Zhang, L. et al.
**摘要**: 研究通过大肠杆菌表达系统优化重组Mb的产量，采用His标签纯化技术，获得高纯度蛋白并验证其氧结合活性，为后续结构研究提供基础。
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2. **文献名称**: *Structural Insights into Mutant Myoglobin’s Role in Cardiomyopathy*
**作者**: Smith, J.R. & Tanaka, M.
**摘要**: 通过X射线晶体学解析重组Mb突变体(R139G)的三维结构，揭示其与遗传性心肌病的关联，阐明了异常氧释放导致细胞损伤的分子机制。
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3. **文献名称**: *Recombinant Myoglobin as a Biosensor for Real-Time Oxygen Monitoring*
**作者**: Gupta, S. et al.
**摘要**: 开发基于荧光标记重组Mb的体外氧传感系统，证明其在低氧微环境检测中的应用潜力，灵敏度达nM级别，适用于肿瘤模型研究。
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4. **文献名称**: *Comparative Analysis of Mammalian Myoglobin Expression in Yeast*
**作者**: Müller, F. et al.
**摘要**: 对比毕赤酵母与酿酒酵母系统表达重组Mb的效率，发现毕赤酵母的糖基化修饰更接近天然蛋白功能，为规模化生产提供优化策略。
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注：以上文献为示例性质，实际引用时需检索PubMed/Web of Science等数据库获取真实信息。
**Background of Recombinant Mb Protein**
Myoglobin (Mb), a small globular protein predominantly found in muscle tissues, plays a critical role in oxygen storage and transport. Comprising a single polypeptide chain (∼17 kDa) bound to a heme prosthetic group, Mb facilitates oxygen diffusion in muscle cells under hypoxic conditions. Its high oxygen-binding affinity and structural simplicity have made it a model system for studying protein folding, ligand-binding dynamics, and evolutionary adaptations in vertebrates.
The advent of recombinant DNA technology revolutionized Mb production. Recombinant Mb is synthesized by inserting the Mb gene into expression vectors (e.g., *E. coli* or yeast systems), enabling scalable, cost-effective production with high purity. This approach circumvents ethical and practical limitations of isolating Mb from animal tissues while allowing precise modifications (e.g., site-directed mutagenesis) to probe structure-function relationships or engineer novel properties.
Recombinant Mb has diverse applications. In biomedical research, it serves as a tool to study oxidative stress, ischemia-reperfusion injury, and oxygen-dependent signaling. Modified variants are explored as oxygen-therapeutic agents or biosensors. In biotechnology, Mb’s stability and solubility make it a candidate for oxygen-carrying additives in cell culture systems or bioartificial tissues. Additionally, recombinant Mb is used in industrial enzymology and as a scaffold for designing metalloenzymes.
Recent advances in synthetic biology and protein engineering have expanded its utility, including fusion proteins for targeted drug delivery and fluorescent Mb derivatives for real-time oxygen imaging. Despite its simplicity, recombinant Mb remains a versatile molecule bridging fundamental science and translational innovation.
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