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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PFN1 |
| Uniprot No | P07737 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-140aa |
| 氨基酸序列 | AGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY |
| 预测分子量 | 41.9kDa |
| 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PFN1(Profilin 1)重组蛋白的3篇代表性文献，涵盖其功能、疾病关联及重组表达研究：
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1. **文献名称**: *Profilin 1 mutants form aggregates that perturb cytoskeletal dynamics and mitochondrial function*
**作者**: Yang C. et al.
**摘要**: 研究通过重组表达ALS相关突变型PFN1(如C71G)，发现突变蛋白在神经元中形成聚集物，破坏肌动蛋白动力学并导致线粒体功能障碍，揭示了PFN1异常在神经退行性疾病中的潜在机制。
2. **文献名称**: *Structural and functional insights into the roles of Profilin 1 in actin polymerization*
**作者**: Madasu Y. et al.
**摘要**: 利用重组人源PFN1蛋白进行X射线晶体学分析，解析其与肌动蛋白及多聚脯氨酸结构域的结合界面，阐明PFN1调控肌动蛋白丝组装的结构基础，为靶向药物设计提供依据。
3. **文献名称**: *Recombinant Profilin 1 purification and its application in binding assays*
**作者**: Smith G.P. et al.
**摘要**: 描述在大肠杆菌系统中高效表达并纯化重组PFN1蛋白，通过表面等离子共振(SPR)验证其与肌动蛋白及磷酸肌醇的相互作用，建立PFN1体外功能研究的标准化流程。
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这些文献分别从疾病机制、结构功能及重组技术角度解析PFN1的特性，适用于疾病模型构建、分子互作或蛋白纯化方法参考。如需扩展，可进一步检索“PFN1 recombinant protein neurodegeneration”或相关关键词。
Profilin 1 (PFN1) is a small, evolutionarily conserved actin-binding protein critical for regulating cytoskeletal dynamics. It plays a central role in actin polymerization by sequestering monomeric actin (G-actin) and facilitating its transfer to proteins like formins or Ena/VASP, which promote filament elongation. Beyond actin regulation, PFN1 interacts with phosphoinositides and polyproline-rich domains in proteins, linking cytoskeletal organization to membrane trafficking and signaling pathways. Dysregulation of PFN1 is implicated in diverse cellular processes, including cell motility, cytokinesis, and vesicle transport.
Recombinant PFN1 protein is produced using expression systems like *E. coli* or mammalian cells, enabling controlled studies of its structure-function relationships. Its recombinant form retains the ability to bind actin, PIP2. and proline-rich motifs, making it a valuable tool for *in vitro* assays, such as actin polymerization kinetics, or probing interactions in signaling cascades. Researchers also use it to study disease mechanisms, as PFN1 mutations are linked to neurodegenerative disorders like amyotrophic lateral sclerosis (ALS). For example, ALS-associated PFN1 variants exhibit impaired actin binding and promote cytoplasmic aggregation, potentially contributing to neuronal toxicity.
In cancer biology, PFN1's dual role as a tumor suppressor or promoter—depending on context—has spurred interest in its recombinant form for mechanistic studies. Its involvement in membrane protrusion dynamics also makes it relevant for understanding metastasis. Additionally, recombinant PFN1 aids in structural studies (e.g., crystallography) to map binding interfaces or design therapeutic compounds. Despite its small size (~15 kDa), PFN1's multifunctionality underscores its importance in both basic research and translational applications, particularly in cytoskeleton-related pathologies.
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