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| 纯度 | >85%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | PIGF |
| Uniprot No | P49764 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-158aa |
| 氨基酸序列 | VHSQGALSAGNNSTEVEVVPFNEVWGRSYCRPMEKLVYILDEYPDEVSHI FSPSCVLLSRCSGCCGDEGLHCVPIKTANITMQILKIPPNRDPHFYVEMT FSQDVLCECRPILETTKAERRKTKGKRKRSRNSQTEEPHP |
| 预测分子量 | 16 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. |
1. **《Recombinant placental growth factor-1 (PlGF-1) improves revascularization in murine models of ischemia》**
- 作者：Luttun A等
- 摘要：研究通过大肠杆菌表达重组PlGF-1蛋白，验证其在缺血模型中促进血管新生和侧支循环形成的能力，证实其作为治疗缺血性疾病的潜力。
2. **《Placenta growth factor is overexpressed and regulates angiogenesis in human endometrial cancer》**
- 作者：De Falco S等
- 摘要：报道PlGF在子宫内膜癌中高表达，通过重组蛋白实验证明其通过VEGFR-1信号通路促进肿瘤血管生成，提示其作为癌症治疗靶点的可能性。
3. **《Role of PlGF in the intra- and intermolecular cross talk between VEGF receptors》**
- 作者：Autiero M等
- 摘要：揭示重组PlGF蛋白通过与VEGF形成异源二聚体，增强VEGFR-1和VEGFR-2的协同激活机制，阐明其在病理性血管生成中的调控作用。
4. **《Recombinant PlGF-2 inhibits pulmonary hypertension by targeting BMPR2 signaling》**
- 作者：Zhou S等
- 摘要：利用哺乳动物细胞表达系统制备PlGF-2重组蛋白，发现其通过调控BMPR2通路改善肺动脉高压模型中的血管重塑，提出新型治疗策略。
**Background of PIGF Recombinant Protein**
Placental Growth Factor (PIGF), a member of the vascular endothelial growth factor (VEGF) family, plays a critical role in angiogenesis and vasculogenesis. It primarily binds to VEGF receptor-1 (VEGFR-1/Flt-1), triggering signaling pathways that regulate endothelial cell proliferation, migration, and survival. Unlike VEGF-A, which is essential for developmental and pathological angiogenesis, PIGF is more selectively involved in pathological conditions, such as ischemia, inflammation, and tumor growth. Its expression is upregulated in diseases like cancer, atherosclerosis, and diabetic retinopathy, making it a potential therapeutic target.
Recombinant PIGF proteins are engineered using genetic modification techniques, often expressed in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian cells) to ensure proper folding and post-translational modifications. These proteins retain the functional activity of native PIGF, enabling researchers to study its biological mechanisms or develop therapeutic strategies. For instance, PIGF inhibitors (e.g., antibodies targeting PIGF) have been explored to block pathological angiogenesis in cancers, while recombinant PIGF itself may aid in tissue repair by promoting vascular regeneration.
In research, recombinant PIGF is widely used to investigate its interactions with co-receptors (e.g., neuropilins) and its role in cross-talk between VEGF family members. Studies also explore its contribution to inflammatory responses by recruiting macrophages and other immune cells. Despite mixed outcomes in clinical trials targeting PIGF, its distinct signaling pathways continue to offer insights for precision therapies. Overall, recombinant PIGF remains a vital tool for dissecting angiogenesis-related diseases and advancing biomedical applications.
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