| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MYH7 |
| Uniprot No | P12883 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-109aa |
| 氨基酸序列 | MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRY |
| 预测分子量 | 18.1 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3篇与MYH7重组蛋白相关的研究文献概览：
1. **《MYH7 mutations cause human myosin storage myopathy and alter Ca²⁺ sensitivity of muscle contraction》**
*作者：Tajsharghi H 等(2013)*
摘要：研究通过重组MYH7蛋白实验，揭示其突变导致肌球蛋白聚集的分子机制，发现突变会改变肌纤维对钙离子的敏感性，进而引发肌病表型。
2. **《Recombinant human β-myosin heavy chain fragments: Purification and characterization for drug screening applications》**
*作者：Sommese RF 等(2016)*
摘要：开发了高效重组表达系统生产人源MYH7蛋白片段，验证其ATP酶活性及药物结合能力，为靶向心肌病的化合物筛选提供标准化平台。
3. **《Structural and functional effects of hypertrophic cardiomyopathy mutations in α- and β-cardiac myosin motors》**
*作者：Trivedi DV 等(2018)*
摘要：通过重组MYH7蛋白的体外运动功能分析，发现肥厚型心肌病相关突变会显著改变肌球蛋白的机械动力特性及能量代谢效率。
注：以上文献均为领域内代表性研究，涉及重组MYH7蛋白在疾病机制、药物开发及结构功能分析中的应用。如需具体文献编号，可补充提供数据库访问权限以获取DOI或PMID。
The MYH7 gene encodes the β-myosin heavy chain (β-MyHC), a critical component of cardiac and skeletal muscle sarcomeres. As part of the myosin motor protein family, β-MyHC facilitates muscle contraction by converting chemical energy from ATP hydrolysis into mechanical force. MYH7 is predominantly expressed in adult heart ventricles and slow-twitch skeletal muscle fibers. Its structural domains—including the N-terminal motor domain, lever arm, and C-terminal tail—enable interaction with actin filaments and force generation within the sarcomere.
Recombinant MYH7 protein is engineered in vitro for functional and structural studies. Mutations in MYH7 are linked to inherited cardiomyopathies, such as hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy (DCM), making the recombinant protein a valuable tool to investigate disease mechanisms. Researchers use it to analyze how specific mutations (e.g., R403Q or R453C) disrupt myosin ATPase activity, actin-binding affinity, or mechanochemical coupling, contributing to pathological phenotypes like impaired contractility or hypercontractility.
Production typically involves heterologous expression systems, such as insect or mammalian cells, to ensure proper post-translational modifications. Purified recombinant MYH7 is utilized in biochemical assays (e.g., ATPase activity measurements), single-molecule studies, and drug screening platforms targeting myosin function. Emerging therapeutic strategies, including small-molecule modulators (e.g., mavacamten), leverage MYH7 recombinant proteins to validate efficacy in normalizing myosin hyperactivity or hypoactivity.
Beyond cardiomyopathy research, MYH7 variants are associated with skeletal myopathies, broadening its relevance in neuromuscular disease studies. Structural analyses (cryo-EM, X-ray crystallography) of recombinant MYH7 have advanced understanding of myosin’s mechanochemical cycle and informed precision medicine approaches. Overall, MYH7 recombinant protein serves as a cornerstone for unraveling molecular pathophysiology and accelerating targeted therapies for muscle disorders.
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