纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | PFN2 |
Uniprot No | P35080 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-140aa |
氨基酸序列 | MAGWQSYVDNLMCDGCCQEAAIVGYCDAKYVWAATAGGVFQSITPIEIDM IVGKDREGFFTNGLALGAKKCSVIRDSLYVDGDCTMDIRTKSQGGEPTYN VAVGRAGRVLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF |
预测分子量 | 15 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PFN2重组蛋白的3篇参考文献及其摘要概括:
1. **文献名称**:*Profilin-2 regulates exosome production by controlling actin dynamics*
**作者**:Chen H. et al.
**摘要**:该研究利用重组PFN2蛋白,揭示了其在调控细胞外泌体分泌中的作用。通过体外实验发现,PFN2通过与肌动蛋白相互作用,影响细胞骨架重组,从而调节囊泡运输和分泌过程。
2. **文献名称**:*Structural insights into the function of profilin-2 in neuronal development*
**作者**:Wang L. et al.
**摘要**:作者通过表达重组PFN2蛋白并结合X射线晶体学分析,解析了其三维结构,发现其C端结构域对神经元突触形成具有关键作用,为PFN2在神经发育中的功能提供了分子机制解释。
3. **文献名称**:*PFN2重组蛋白在乳腺癌细胞迁移中的功能研究*
**作者**:Zhang Y. et al.
**摘要**:研究利用大肠杆菌表达系统获得高纯度PFN2重组蛋白,发现其过表达可抑制乳腺癌细胞的侵袭和迁移,机制可能与抑制RhoA/ROCK信号通路及肌动蛋白纤维重塑有关。
注:以上文献信息为示例,实际文献需通过数据库(如PubMed)检索确认。如需具体文章,建议以“PFN2 recombinant protein”或“Profilin-2 expression”为关键词进行查询。
**Background of PFN2 Recombinant Protein**
Profilin-2 (PFN2) is a member of the profilin family of small actin-binding proteins that play pivotal roles in regulating cytoskeletal dynamics. Unlike its ubiquitously expressed isoform, profilin-1 (PFN1), PFN2 is predominantly expressed in the brain, testis, and certain cancer cells, suggesting specialized functions in neuronal development, synaptic plasticity, and disease pathogenesis. PFN2 modulates actin polymerization by sequestering monomeric actin (G-actin) and interacting with proline-rich domains of proteins like formins and Ena/VASP, thereby influencing cell motility, vesicle trafficking, and membrane remodeling.
The recombinant PFN2 protein is engineered using *in vitro* expression systems (e.g., *E. coli* or mammalian cells) to ensure high purity and bioactivity. Its production enables researchers to study PFN2-specific mechanisms independent of PFN1. which shares ~80% sequence homology but exhibits distinct functional and regulatory properties. For instance, PFN2 has been linked to neurodevelopmental disorders, such as autism spectrum disorders, and neurodegenerative diseases, including Alzheimer’s, where actin dysregulation contributes to synaptic dysfunction. In cancer, PFN2 may act as a tumor suppressor or promoter depending on context, influencing metastasis and cytoskeletal reorganization.
Recombinant PFN2 is widely utilized in *in vitro* assays, structural studies, and therapeutic exploration. Its applications include elucidating actin-binding kinetics, screening for interaction partners, and developing targeted therapies for cytoskeleton-related diseases. Ongoing research aims to clarify its role in cellular signaling pathways and potential as a diagnostic or therapeutic biomarker.
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