| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PFN3 |
| Uniprot No | P60673 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-137aa |
| 氨基酸序列 | MGDWKVYISA VLRDQRIDDV AIVGHADNSC VWASRPGGLL AAISPQEVGV LTGPDRHTFL QAGLSVGGRR CCVIRDHLLA EGDGVLDART KGLDARAVCV GRAPRALLVL MGRRGVHGGI LNKTVHELIR GLRMQGA |
| 预测分子量 | 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. |
以下为模拟生成的关于PFN3重组蛋白的参考文献示例(注：实际文献可能需要通过学术数据库验证)：
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1. **标题**：*Recombinant PFN3 Expression in E. coli and Its Role in Actin Polymerization*
**作者**：Zhang, L. et al.
**摘要**：本研究成功构建了PFN3重组蛋白的原核表达系统，通过大肠杆菌表达并纯化具有生物活性的PFN3蛋白。实验表明，重组PFN3能显著抑制肌动蛋白的聚合，提示其在细胞骨架调控中的潜在作用。
2. **标题**：*Profilin-3 (PFN3) Recombinant Protein Suppresses Tumor Cell Invasion via VEGF Signaling Pathway*
**作者**：Wang, Y. et al.
**摘要**：通过哺乳动物细胞体系表达重组PFN3蛋白，发现其过表达可抑制肝癌细胞的侵袭能力。机制研究表明，PFN3通过下调VEGF信号通路影响肿瘤微环境的血管生成。
3. **标题**：*Structural Characterization of Human PFN3 Recombinant Protein by X-ray Crystallography*
**作者**：Smith, J.R. et al.
**摘要**：首次解析了重组人源PFN3蛋白的晶体结构，揭示了其与PFN家族其他成员(如PFN1)的结构差异，并探讨了其特异性结合多聚脯氨酸区域的分子基础。
4. **标题**：*PFN3 Recombinant Protein Enhances Neurite Outgrowth in Cortical Neurons*
**作者**：Chen, H. et al.
**摘要**：利用真核表达系统制备重组PFN3蛋白，发现其能促进原代皮层神经元的突触生长，提示PFN3可能在神经发育或再生医学中具有应用潜力。
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建议通过PubMed或Web of Science搜索**"PFN3 recombinant"**或**"Profilin3 expression"**获取真实文献。如需具体文献协助，请提供更多上下文。
**Background of PFN3 Recombinant Protein**
Profilin-3 (PFN3) is a member of the profilin family of actin-binding proteins, which play critical roles in regulating cytoskeletal dynamics by interacting with actin monomers and polyproline-rich proteins. Unlike its well-studied paralogs, PFN1 and PFN2. PFN3 exhibits tissue-specific expression, with higher levels observed in reproductive organs, the nervous system, and certain cancer cells. Its precise biological functions remain less defined, though emerging studies suggest involvement in clathrin-mediated endocytosis, vesicle trafficking, and cell motility. PFN3 is also implicated in pathological processes, including tumor progression and neurodegenerative disorders, though mechanistic insights are limited.
Recombinant PFN3 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional protein for structural and functional studies. This allows researchers to dissect PFN3’s unique binding properties, such as its affinity for actin isoforms or phosphoinositides, and its regulatory interplay with ligands like VASP or formins. Structural analyses reveal conserved profilin motifs but distinct surface charge distributions, potentially explaining functional divergence from other profilins.
Interest in PFN3 has grown due to its paradoxical roles in cancer: while PFN1 often acts as a tumor suppressor, PFN3 may promote invasiveness in specific malignancies, such as prostate cancer. Recombinant PFN3 facilitates *in vitro* assays to map interaction networks and screen for therapeutic modulators. Additionally, it aids in exploring its neuroprotective or pathogenic contributions in models of Alzheimer’s or Huntington’s disease.
Despite progress, key questions persist regarding PFN3’s context-dependent functions and post-translational modifications. Recombinant protein tools remain essential for resolving these ambiguities and advancing translational applications in precision medicine.
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