| 纯度 | ＞90% by SDS-PAGE |
| 种属 | Human |
| 靶点 | ACTA2 |
| Uniprot No | P62736 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 3-377aa |
| 氨基酸序列 | EEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF |
| 预测分子量 | 47.8 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ACTA2重组蛋白的3篇参考文献及摘要概括：
1. **文献名称**: "Recombinant human α-smooth muscle actin: production and structural analysis"
**作者**: Moriyama K, et al.
**摘要**: 该研究利用大肠杆菌表达系统成功表达并纯化了重组人源ACTA2(α-SMA)蛋白，通过圆二色谱和X射线晶体学分析了其二级结构和三维构象，验证了其与天然蛋白的结构相似性。
2. **文献名称**: "Functional characterization of recombinant ACTA2 mutants in vascular smooth muscle cells"
**作者**: Guo DC, et al.
**摘要**: 通过构建ACTA2基因突变体重组蛋白，研究其在血管平滑肌细胞中的聚合能力及收缩功能，发现特定突变导致细胞骨架异常，揭示了ACTA2突变与主动脉疾病的关联机制。
3. **文献名称**: "Purification and application of recombinant α-smooth muscle actin in fibrosis models"
**作者**: Hinz B, et al.
**摘要**: 报道了从哺乳动物细胞中高效纯化重组ACTA2蛋白的方法，并证明其在体外纤维化模型中促进肌成纤维细胞活化的作用，为研究组织纤维化提供了工具。
(注：以上文献信息为模拟示例，实际引用需核对真实数据库。)
**Background of ACTA2 Recombinant Protein**
ACTA2. encoding α-smooth muscle actin (α-SMA), is a critical cytoskeletal protein predominantly expressed in vascular smooth muscle cells (VSMCs) and myofibroblasts. As a marker of the contractile phenotype, α-SMA plays a central role in maintaining vascular tone, tissue elasticity, and mechanical stability. It polymerizes into microfilaments, interacting with myosin to facilitate cell contraction and motility. Dysregulation of ACTA2 is implicated in vascular pathologies, including aortic aneurysms, atherosclerosis, and fibrosis, as well as cancers characterized by aberrant cell migration.
Recombinant ACTA2 protein is engineered using expression systems like *E. coli* or mammalian cells, enabling large-scale production of high-purity α-SMA for research and therapeutic development. Its applications span *in vitro* studies exploring VSMC differentiation, drug screening for anti-fibrotic or anti-cancer therapies, and mechanistic investigations of vascular remodeling. Mutations in ACTA2 (e.g., R179 substitutions) are linked to hereditary vascular disorders, making the recombinant protein valuable for modeling disease-associated pathways.
In regenerative medicine, α-SMA-expressing cells are essential for engineered tissues requiring contractile function. Despite its utility, challenges remain in mimicking post-translational modifications critical for native protein behavior. Ongoing advances in recombinant technology aim to enhance bioactivity, positioning ACTA2 as a pivotal tool in understanding and targeting smooth muscle-related diseases.
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