| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MYH9 |
| Uniprot No | P35579 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-241aa |
| 氨基酸序列 | AQQAADKYLYVDKNFINNPLAQADWAAKKLVWVPSDKSGFEPASLKEEVGEEAIVELVENGKKVKVNKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI |
| 预测分子量 | 54.2kDa |
| 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MYH9重组蛋白的3篇参考文献示例(注：文献信息为模拟概括，实际引用请核实具体来源)：
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1. **文献名称**: "Expression and Functional Analysis of Recombinant MYH9 in Platelet Disorders"
**作者**: Smith A, et al.
**摘要**: 本研究成功在大肠杆菌系统中表达了重组MYH9蛋白，并验证其与肌动蛋白的相互作用。通过体外实验发现，MYH9突变体导致细胞迁移缺陷，揭示了其在遗传性血小板疾病中的分子机制。
2. **文献名称**: "Structural Characterization of MYH9 Recombinant Protein Using Cryo-EM"
**作者**: Li X, et al.
**摘要**: 利用冷冻电镜技术解析了重组MYH9蛋白的分子结构，发现其头部结构域的关键ATP酶活性位点，为靶向MYH9相关疾病的药物设计提供了结构基础。
3. **文献名称**: "MYH9 Reconstitution Rescues Cytokinesis Defects in Cancer Cells"
**作者**: Tanaka K, et al.
**摘要**: 通过重组MYH9蛋白回补实验，证明其在癌细胞胞质分裂中的作用，MYH9缺失导致分裂失败，而外源蛋白可恢复正常表型，提示其作为癌症治疗靶点的潜力。
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**注意**：以上内容为学术文献的模拟概括，实际文献需通过PubMed、Web of Science等数据库检索确认。如需具体文献，建议以“MYH9 recombinant protein”为关键词结合研究领域(如细胞生物学、血液病学)进一步筛选。
MYH9 recombinant protein is derived from the MYH9 gene, which encodes the non-muscle myosin heavy chain IIA (NMMHC-IIA), a critical cytoskeletal motor protein. Belonging to the myosin superfamily, MYH9 plays essential roles in cell motility, structural maintenance, and cytokinesis by interacting with actin filaments through ATP-dependent mechanochemical activity. Structurally, it consists of an N-terminal motor domain (for actin binding and ATP hydrolysis), a regulatory α-helical neck region, and a C-terminal tail involved in dimerization and cargo binding.
Mutations in MYH9 are linked to MYH9-related disorders (MYH9-RD), a group of autosomal-dominant conditions characterized by macrothrombocytopenia, hearing loss, glomerulonephritis, and cataracts. These pathogenic variants often disrupt myosin assembly, impairing platelet formation and cellular biomechanics. Beyond genetic diseases, MYH9 dysregulation is associated with cancer progression, renal dysfunction, and fibrosis, highlighting its broad pathophysiological relevance.
Recombinant MYH9 protein is typically produced in heterologous systems (e.g., bacterial, insect, or mammalian cells) using plasmid vectors that enable controlled expression. Purification often involves affinity chromatography (e.g., His-tag or GST-tag systems) followed by refolding or cleavage steps to ensure functional integrity. Researchers utilize this recombinant protein to study MYH9’s molecular interactions, screen therapeutic compounds targeting myosin activity, and model disease mechanisms in vitro. Its applications extend to developing diagnostic tools for MYH9-RD and exploring targeted therapies to correct cytoskeletal defects. As a standardized reagent, recombinant MYH9 enhances reproducibility in studies dissecting cytoskeletal dynamics and its role in human diseases.
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