首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PGF |
| Uniprot No | P49763 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-170aa |
| 氨基酸序列 | LPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCRALERLVDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSGDRPSYVELTFSQHVRCECRPLREKMKPERRRPKGRGKRRREKQRPTDCHLCGDAVPRR |
| 预测分子量 | 45.1 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. |
以下是基于现有研究方向的模拟参考文献示例(请注意，具体文献需通过学术数据库核实)：
1. **文献名称**：重组人胎盘生长因子(PGF)在大肠杆菌中的高效表达与纯化
**作者**：张磊等
**摘要**：本研究构建了人PGF基因原核表达载体，通过大肠杆菌系统实现高效表达，并利用亲和层析技术获得高纯度重组蛋白，为后续功能研究奠定基础。
2. **文献名称**：PGF重组蛋白促进血管生成的体外实验研究
**作者**：Chen Y, et al.
**摘要**：通过哺乳动物细胞表达系统制备重组PGF，证实其可显著增强内皮细胞增殖、迁移及管状结构形成，提示其在缺血性疾病治疗中的潜在应用价值。
3. **文献名称**：重组PGF与VEGF协同调控肿瘤血管生成的分子机制
**作者**：Smith J, et al.
**摘要**：研究发现重组PGF蛋白通过激活特定信号通路，与VEGF协同促进肿瘤血管异常增生，为抗肿瘤血管联合疗法提供新靶点。
4. **文献名称**：基于重组PGF蛋白的妊娠相关疾病诊断试剂开发
**作者**：王芳等
**摘要**：利用真核表达的重组PGF蛋白制备单克隆抗体，成功建立妊娠子痫前期血清学检测方法，具有较高临床灵敏度与特异性。
注：以上为基于领域知识的模拟数据，实际文献请通过PubMed、Web of Science等平台以"recombinant placental growth factor"等关键词检索。建议结合具体研究方向(如疾病模型、生产工艺等)进一步筛选文献。
Placental growth factor (PGF), a member of the vascular endothelial growth factor (VEGF) family, is a secreted glycoprotein initially identified for its role in placental vasculogenesis during embryonic development. Structurally, it shares homology with VEGF-A but exhibits distinct receptor binding preferences, primarily interacting with VEGFR-1 (Flt-1) and neuropilin co-receptors. Unlike VEGF-A’s strong pro-angiogenic effects, PGF modulates vascular remodeling by fine-tuning VEGF signaling pathways, influencing endothelial cell migration, and promoting collateral blood vessel formation under ischemic conditions.
The recombinant PGF protein, produced through genetic engineering in systems like mammalian cells (e.g., CHO) or *E. coli*, retains these biological activities while offering standardized quality for research and therapeutic applications. Its production involves cloning the PGF gene into expression vectors, followed by purification steps to ensure >95% purity. This recombinant form enables precise studies of PGF’s mechanisms in pathological angiogenesis, particularly in cancer, where it contributes to tumor vascularization and metastasis, and in cardiovascular diseases, where it may enhance compensatory blood flow.
Clinically, recombinant PGF has shown potential in tissue repair and ischemic disease models. Paradoxically, both PGF supplementation and inhibition strategies are being explored: enhancing PGF may improve perfusion in peripheral artery disease, while blocking it could starve tumors. Additionally, its involvement in inflammatory pathways links it to conditions like diabetic retinopathy and rheumatoid arthritis.
As a research tool, recombinant PGF aids in decoding crosstalk between angiogenic factors and stromal cells. Despite promising preclinical data, clinical translation remains limited, underscoring the need for deeper mechanistic insights. The development of isoform-specific recombinant proteins (e.g., PGF-2) continues to refine its therapeutic targeting, positioning PGF as a versatile modulator in vascular biology and precision medicine.
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