| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPM1 |
| Uniprot No | P09493 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-284aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMDAIKKKMQMLKLDKENALDRAEQAEADKK AAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI ESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE ERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSD KLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALND MTSM |
| 预测分子量 | 35 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. |
以下是与TPM1重组蛋白相关的3篇参考文献示例(注：内容为模拟概括，非真实文献)：
1. **《重组TPM1蛋白在大肠杆菌中的表达与结构分析》**
作者：Smith A et al.
摘要：研究通过原核表达系统成功表达并纯化了人源TPM1重组蛋白，利用X射线晶体学解析其三维结构，揭示了TPM1与肌动蛋白结合的特定结构域。
2. **《TPM1重组蛋白在肿瘤细胞迁移中的功能研究》**
作者：Zhang L et al.
摘要：通过体外实验证实，TPM1重组蛋白的过表达可显著抑制乳腺癌细胞的侵袭和迁移能力，提示其在癌症治疗中的潜在应用价值。
3. **《TPM1基因突变体重组蛋白的生化特性与心肌病关联》**
作者：Johnson R et al.
摘要：构建了TPM1基因突变型重组蛋白，发现其与野生型相比肌钙蛋白结合能力下降，为遗传性心肌病的分子机制提供了实验依据。
**Background of TPM1 Recombinant Protein**
TPM1 (tropomyosin 1) is a member of the tropomyosin family of actin-binding proteins, playing critical roles in stabilizing cytoskeletal structures and regulating muscle contraction. Encoded by the *TPM1* gene, it generates multiple isoforms through alternative splicing, which are expressed in muscle and non-muscle tissues. These isoforms, such as TPM1α and TPM1κ, exhibit tissue-specific functions, including modulating actin filament dynamics, cell motility, and intracellular trafficking. Dysregulation of TPM1 is linked to cardiovascular diseases, muscular disorders, and cancer metastasis, highlighting its biological significance.
Recombinant TPM1 protein is produced using biotechnological platforms like *E. coli* or mammalian expression systems, enabling large-scale synthesis of purified, functional protein for research. Its production involves cloning the *TPM1* gene into expression vectors, followed by transfection, protein expression, and purification via affinity chromatography. Recombinant TPM1 retains native structural and functional properties, making it valuable for *in vitro* studies.
In research, TPM1 recombinant protein is widely used to investigate mechanisms of cytoskeletal regulation, muscle contraction, and disease pathogenesis. It serves as a tool to study interactions with actin, myosin, and other regulatory proteins, aiding in drug discovery for conditions like hypertrophic cardiomyopathy or cancer. Additionally, it supports the development of diagnostic assays and therapeutic strategies targeting TPM1-associated pathways.
Overall, TPM1 recombinant protein is a pivotal resource for advancing understanding of cellular mechanics and disease mechanisms, bridging molecular biology with clinical applications.
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