| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MYLPF |
| Uniprot No | Q96A32 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-169aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAPKRAKRRTVEGGSSSVFSMFDQTQIQEF KEAFTVIDQNRDGIIDKEDLRDTFAAMGRLNVKNEELDAMMKEASGPINF TVFLTMFGEKLKGADPEDVITGAFKVLDPEGKGTIKKKFLEELLTTQCDR FSQEEIKNMWAAFPPDVGGNVDYKNICYVITHGDAKDQE |
| 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MYLPF重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Expression and functional characterization of recombinant MYLPF in smooth muscle contraction"*
**作者**：Chen L, et al.
**摘要**：该研究通过大肠杆菌系统成功表达并纯化了重组MYLPF蛋白，证实其在体外能显著增强平滑肌肌球蛋白的磷酸酶活性，揭示了MYLPF通过调控肌球蛋白轻链去磷酸化参与平滑肌收缩的分子机制。
2. **文献名称**：*"Structural insights into MYLPF regulatory subunit interactions using recombinant protein technology"*
**作者**：Wang Y, et al.
**摘要**：利用重组MYLPF蛋白进行X射线晶体学分析，解析了MYLPF与肌球蛋白磷酸酶催化亚基的结合界面，发现其C端结构域是维持复合物稳定性的关键区域，为开发靶向抑制剂提供了结构基础。
3. **文献名称**：*"Recombinant MYLPF suppresses cancer cell migration by modulating actomyosin dynamics"*
**作者**：Kimura T, et al.
**摘要**：研究通过昆虫细胞表达系统获得高纯度重组MYLPF，体外实验表明其可通过抑制RhoA/ROCK通路降低肿瘤细胞伪足形成和迁移能力，提示MYLPF在癌症转移中的潜在治疗价值。
注：上述文献为虚拟示例，实际文献需通过学术数据库检索。建议结合具体研究方向补充关键词(如“重组表达”“功能分析”“疾病模型”)进一步筛选。
MYLPF (Myosin Light Chain Phosphatase regulatory subunit F), also known as myosin phosphatase target subunit 1 (MYPT1), is a critical regulatory component of the myosin light chain phosphatase (MLCP) complex. This protein plays a central role in modulating smooth muscle contraction and non-muscle cell motility by regulating the dephosphorylation of myosin light chain (MLC), a process essential for actin-myosin interaction. MYLPF acts as a scaffold that binds the catalytic subunit of protein phosphatase 1 (PP1c) and myosin, enabling targeted dephosphorylation of MLC to promote muscle relaxation or reduce contractile force.
Structurally, MYLPF contains conserved domains such as the N-terminal PP1c-binding motif, central coiled-coil regions for dimerization, and C-terminal sequences for myosin interaction. Its activity is tightly regulated by post-translational modifications, including phosphorylation by Rho-associated kinase (ROCK) and other kinases, which inhibit MLCP function and enhance myosin activation. Dysregulation of MYLPF has been implicated in cardiovascular diseases (e.g., hypertension, atherosclerosis), cancer metastasis (via altered cell migration), and neurological disorders.
Recombinant MYLPF proteins are widely used to study MLCP signaling mechanisms, screen therapeutic compounds targeting muscle hypercontractility, and model disease-related mutations. Produced in bacterial or mammalian expression systems, these proteins retain functional domains for biochemical assays, structural studies, and drug discovery. However, challenges in maintaining solubility and post-translational modification fidelity necessitate optimization of expression conditions. Current research leverages recombinant MYLPF to dissect its role in cytoskeletal dynamics and develop precision therapies for conditions linked to MLCP dysregulation.
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