| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CFL2 |
| Uniprot No | Q9Y281 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-166aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMASGVTVNDEVIKVFNDMKVRKSSTQEEIK KRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDC RYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTG IKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPL |
| 预测分子量 | 21 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CFL2(Cofilin-2)重组蛋白的模拟参考文献示例，供参考：
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1. **文献名称**：*High-Yield Expression and Purification of Recombinant Human Cofilin-2 in Bacterial Systems*
**作者**：Chen X, Wang Y, et al.
**摘要**：本研究优化了人源CFL2基因在大肠杆菌中的表达条件，采用亲和层析技术高效纯化重组蛋白，并通过体外肌动蛋白解聚实验证实其功能活性，为后续结构及机制研究提供材料基础。
2. **文献名称**：*Functional Role of Recombinant Cofilin-2 in Skeletal Muscle Regeneration*
**作者**：Müller R, Schmidt T, et al.
**摘要**：通过体外表达重组CFL2蛋白，探究其对肌管细胞中肌动蛋白动态的调控作用，发现CFL2缺失会导致肌纤维形成障碍，提示其在肌肉再生中的关键角色。
3. **文献名称**：*Crystal Structure Analysis of Recombinant Cofilin-2 Reveals Actin-Binding Mechanisms*
**作者**：Tanaka K, Sato H, et al.
**摘要**：利用X射线晶体学解析重组CFL2的三维结构，结合分子动力学模拟，阐明其与肌动蛋白丝结合的特异性位点及构象变化，为病理突变研究提供结构依据。
4. **文献名称**：*Recombinant CFL2 as a Biomarker in Hypertrophic Cardiomyopathy: In Vitro and Murine Model Studies*
**作者**：Gupta S, Patel V, et al.
**摘要**：在心肌病模型中评估重组CFL2的异常磷酸化水平，发现其与心肌细胞肥大相关，提示CFL2可能作为疾病潜在生物标志物或治疗靶点。
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**说明**：以上文献为模拟示例，实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“recombinant cofilin-2”“CFL2 expression”等获取详细信息。
Cofilin-2 (CFL2) is a member of the cofilin family of actin-binding proteins, primarily expressed in skeletal and cardiac muscles. It plays a critical role in regulating actin filament dynamics by severing and depolymerizing filamentous actin (F-actin), thereby facilitating cytoskeletal reorganization essential for muscle contraction, maintenance, and repair. Unlike its ubiquitously expressed isoform cofilin-1 (CFL1), CFL2 is muscle-specific and is crucial for sarcomere assembly and myofibril stability during muscle development and function.
Structurally, CFL2 contains a conserved actin-depolymerizing factor (ADF) domain that enables its interaction with actin. Its activity is tightly regulated by phosphorylation; LIM kinase-mediated phosphorylation at Ser-3 inhibits its actin-binding ability, while phosphatases reactivate it. Dysregulation of CFL2 is linked to muscle pathologies, including nemaline myopathy and cardiomyopathies, where aberrant actin dynamics impair muscle integrity.
Recombinant CFL2 protein is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, biologically active CFL2 for research. It serves as a tool to study actin dynamics in vitro, investigate muscle-specific cytoskeletal mechanisms, and explore therapeutic strategies for muscle disorders. Recent studies also highlight its potential role in cancer metastasis, as actin remodeling influences cell motility. Recombinant CFL2 thus bridges basic research and translational applications, offering insights into muscle biology and disease mechanisms.
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