| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPM4 |
| Uniprot No | P67936 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-248aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI |
| 预测分子量 | 31 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. |
以下是关于TPM4重组蛋白的3篇参考文献示例(注：内容为模拟示例，实际文献需通过学术数据库检索确认)：
1. **文献名称**：*Expression and purification of recombinant human TPM4 in Escherichia coli*
**作者**：Smith J, et al.
**摘要**：该研究描述了在大肠杆菌系统中高效表达和纯化重组人TPM4蛋白的方法，并验证了其与肌动蛋白结合的功能活性。
2. **文献名称**：*Structural insights into TPM4 reorganization during cytoskeletal remodeling*
**作者**：Lee H, et al.
**摘要**：通过X射线晶体学解析了TPM4重组蛋白的构象变化，揭示了其在细胞骨架动态调节中的分子机制。
3. **文献名称**：*TPM4 overexpression promotes cancer cell invasion via ERK signaling*
**作者**：Wang Y, et al.
**摘要**：研究利用重组TPM4蛋白进行功能实验，证明其通过激活ERK通路增强肿瘤细胞迁移和侵袭能力，提示其作为癌症治疗靶点的潜力。
(提示：实际研究中建议结合PubMed、Web of Science等平台，以关键词“TPM4 recombinant protein”检索最新文献。)
**Background of TPM4 Recombinant Protein**
Tropomyosin 4 (TPM4), a member of the tropomyosin family, is an actin-binding protein critical for regulating cytoskeletal dynamics and contractile functions in eukaryotic cells. Encoded by the *TPM4* gene, it produces multiple isoforms through alternative splicing, which exhibit tissue-specific expression and distinct roles in stabilizing actin filaments, modulating cell motility, and maintaining structural integrity. Unlike other tropomyosin isoforms predominantly found in muscle tissues, TPM4 is widely expressed in non-muscle cells, where it participates in processes such as cytokinesis, cell migration, and intracellular trafficking.
Recombinant TPM4 protein is engineered using molecular cloning techniques, often expressed in bacterial or eukaryotic systems (e.g., *E. coli* or mammalian cells) to ensure proper folding and post-translational modifications. Its production addresses challenges in isolating native TPM4 from tissues, enabling large-scale studies on its biochemical properties, interactions with actin, and regulatory mechanisms. Researchers utilize TPM4 recombinant protein to investigate its role in pathological conditions, particularly cancer, where aberrant TPM4 expression correlates with tumor metastasis, epithelial-mesenchymal transition (EMT), and chemoresistance. For instance, elevated TPM4 levels are linked to enhanced invadopodia formation in invasive cancer cells, promoting extracellular matrix degradation and invasion.
Additionally, TPM4 recombinant protein serves as a tool for developing targeted therapies. Studies explore its potential as a biomarker or therapeutic target, given its involvement in cytoskeletal remodeling pathways critical to disease progression. Despite advances, the isoform-specific functions and regulatory networks of TPM4 remain under investigation, highlighting the need for further structural and functional characterization using recombinant variants. Overall, TPM4 recombinant protein is a vital resource for dissecting cellular mechanics and designing interventions for cytoskeleton-related disorders.
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