纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MYO |
Uniprot No | Q92551 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-441aa |
氨基酸序列 | MCVCQTMEVGQYGKNASRAGDRGVLLEPFIHQVGGHSSMMRYDDHTVCKPLISREQRFYESLPPEMKEFTPEYKGVVSVCFEGDSDGYINLVAYPYVESETVEQDDTTEREQPRRKHSRRSLHRSGSGSDHKEEKASLSLETSESSQEAKSPKVELHSHSEVPFQMLDGNSGLSSEKISHNPWSLRCHKQQLSRMRSESKDRKLYKFLLLENVVHHFKYPCVLDLKMGTRQHGDDASAEKAARQMRKCEQSTSATLGVRVCGMQVYQLDTGHYLCRNKYYGRGLSIEGFRNALYQYLHNGLDLRRDLFEPILSKLRGLKAVLERQASYRFYSSSLLVIYDGKECRAESCLDRRSEMRLKHLDMVLPEVASSCGPSTSPSNTSPEAGPSSQPKVDVRMIDFAHSTFKGFRDDPTVHDGPDRGYVFGLENLISIMEQMRDENQ |
预测分子量 | 66.2kDa |
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MYO重组蛋白的3篇示例文献(虚构内容,仅供参考):
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1. **文献名称**: *Heterologous Expression and Purification of Functional MYO1A in Escherichia coli*
**作者**: Zhang, L.; Chen, W.
**摘要**: 本研究通过优化大肠杆菌表达系统,成功实现人源MYO1A重组蛋白的可溶性表达。采用镍柱亲和层析纯化后,通过ATP酶活性实验验证其功能,为后续肌球蛋白分子机制研究提供可靠工具。
2. **文献名称**: *Cryo-EM Structure of Recombinant MYO6 Reveals Mechanochemical Coupling Mechanism*
**作者**: Ito, K.; Tanaka, R.
**摘要**: 利用冷冻电镜技术解析了重组表达的小鼠MYO6蛋白的原子结构,揭示了其独特的尾端结构域与运动功能偶联机制,为理解遗传性耳聋相关突变位点提供结构基础。
3. **文献名称**: *MYO10 Recombinant Protein Enhances Cellular Migration in Cancer Metastasis Models*
**作者**: Gupta, S.; Patel, A.
**摘要**: 通过杆状病毒系统表达人源MYO10重组蛋白,发现其显著促进肿瘤细胞的定向迁移能力,表明MYO10在癌症转移微环境中的潜在调控作用,提示其作为治疗靶点的可能性。
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注:以上文献为模拟示例,实际研究中请通过PubMed或Web of Science检索真实文献。
MYO recombinant proteins are engineered versions of myosin, a critical motor protein involved in cellular movement, muscle contraction, and intracellular transport. Myosins belong to a large protein superfamily characterized by their ATP-dependent actin-binding activity, enabling mechanical force generation. The term "MYO" typically refers to specific isoforms, such as MYO1 (non-muscle myosin) or MYO7 (associated with hearing loss), depending on their biological context. Recombinant MYO proteins are produced using biotechnological systems like bacterial, insect, or mammalian cell cultures, allowing precise control over protein purity, post-translational modifications, and functional domains.
These proteins have become indispensable tools in biomedical research. Scientists utilize recombinant MYO to study molecular mechanisms of muscle diseases (e.g., cardiomyopathies), cytoskeletal dynamics, and cellular trafficking processes. Their standardized production enables reproducible experiments in structural biology, such as cryo-EM studies to resolve myosin-actin interaction mechanisms. In drug development, MYO variants serve as targets for screening therapeutic compounds aimed at modulating muscle contractility or treating motor protein-related disorders like Usher syndrome.
Recent advances include the engineering of truncated MYO constructs for simplified functional assays and fluorescently tagged versions for live-cell imaging. Challenges persist in replicating native phosphorylation patterns and multi-subunit interactions, driving innovations in expression systems. MYO recombinant proteins also underpin diagnostic applications, including antibody generation for detecting myosin-related biomarkers in cardiovascular diseases. As gene editing and protein engineering technologies evolve, customized MYO proteins are expected to play expanded roles in personalized medicine and mechanobiology research.
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