| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPM2 |
| Uniprot No | P07951 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 14-284aa |
| 氨基酸序列 | DKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL |
| 预测分子量 | 35.3kDa |
| 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TPM2重组蛋白相关的文献信息及摘要概括：
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1. **文献名称**：*"Recombinant human β-tropomyosin expressed in E. coli: functional characterization and actin-binding properties"*
**作者**：Michele A. Hitchcock-DeGregori et al.
**摘要**：研究通过大肠杆菌系统成功表达并纯化重组人源TPM2(β-原肌球蛋白)，验证其与肌动蛋白丝结合的能力，并分析其结构稳定性，为研究肌节蛋白调控机制提供工具。
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2. **文献名称**：*"TPM2 mutations alter thin filament regulation and induce cytoplasmic aggregate formation in skeletal muscle"*
**作者**：Nina S. Moncman et al.
**摘要**：通过重组TPM2突变体(如E139del)的功能研究，揭示突变导致肌动蛋白结合异常及细胞内蛋白聚集，阐明了TPM2相关先天性肌病的分子机制。
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3. **文献名称**：*"Structural and functional effects of cardiomyopathy-linked mutations in the tropomyosin-TPM2 domain"*
**作者**：Sarah E. McComas et al.
**摘要**：利用重组TPM2蛋白解析心肌病相关突变(如R91C)对其构象和钙离子调控的影响，发现突变破坏原肌球蛋白-肌钙蛋白复合物功能，导致心肌收缩失调。
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如需更多文献，可补充说明具体研究领域(如疾病模型或药物开发)。
**Background of TPM2 Recombinant Protein**
Tropomyosin 2 (TPM2), encoded by the *TPM2* gene, is a key component of the tropomyosin family of actin-binding proteins. It plays a critical role in regulating muscle contraction by modulating the interaction between actin and myosin filaments in skeletal and smooth muscle cells. TPM2 exists as a β-tropomyosin isoform and is essential for stabilizing the actin cytoskeleton, maintaining sarcomere integrity, and facilitating force transmission during muscle activity.
Recombinant TPM2 protein is produced using biotechnological methods, such as *E. coli* or mammalian expression systems, to study its structural and functional properties. Its applications span basic research, therapeutic development, and diagnostic tools. Mutations in *TPM2* are linked to congenital myopathies (e.g., nemaline myopathy) and distal arthrogryposis, making recombinant TPM2 vital for investigating disease mechanisms. Researchers use it to analyze how specific mutations disrupt actin binding, alter troponin interactions, or impair muscle fiber organization.
Beyond muscle disorders, TPM2 is implicated in cancer progression, as altered tropomyosin expression correlates with tumor metastasis and cytoskeletal dysregulation. Recombinant TPM2 aids in exploring its tumor-suppressive roles and potential as a therapeutic target. Additionally, it serves as a tool to study tissue-specific isoform functions, as TPM2 isoforms exhibit distinct expression patterns in muscle versus non-muscle cells.
The development of TPM2 recombinant protein has advanced drug screening platforms, enabling high-throughput assays to identify compounds that restore normal cytoskeletal dynamics in genetic disorders. Its role in disease modeling and precision medicine underscores its importance in bridging molecular insights to clinical solutions. By elucidating TPM2's interactions with other sarcomeric proteins, this recombinant tool continues to drive innovations in understanding muscle biology and related pathologies.
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