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. |
以下是关于PGF(胎盘生长因子，Placental Growth Factor)重组蛋白的参考文献示例(内容为虚构，仅供格式参考)：
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1. **文献名称**：Recombinant PGF enhances angiogenesis in ischemic mouse models
**作者**：Chen L, et al.
**摘要**：本研究通过在大肠杆菌中表达重组人PGF蛋白，验证其促进血管内皮细胞迁移和管状结构形成的能力。动物实验表明，局部注射重组PGF可显著改善小鼠后肢缺血模型的血液灌注。
2. **文献名称**：Targeting PlGF with recombinant antibodies inhibits tumor growth
**作者**：Martinez R, et al.
**摘要**：开发了一种抗PGF重组单克隆抗体，并在结直肠癌小鼠模型中验证其疗效。结果显示，抗体通过阻断PGF/VEGFR-1信号通路，抑制肿瘤血管生成并减少转移灶形成。
3. **文献名称**：High-yield production of bioactive PGF in Pichia pastoris
**作者**：Kim S, et al.
**摘要**：优化毕赤酵母表达系统，实现重组PGF的高效分泌表达与纯化。通过体外细胞实验证实，重组蛋白具有与天然PGF相似的生物活性，为大规模临床应用提供可能。
4. **文献名称**：Role of recombinant PGF in preeclampsia pathogenesis
**作者**：Gupta A, et al.
**摘要**：利用重组PGF蛋白探究子痫前期患者胎盘血管功能障碍机制。研究发现，过表达PGF可部分恢复缺氧诱导的滋养层细胞凋亡，提示其作为潜在治疗靶点。
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*注：以上文献及作者为示例性虚构内容，实际研究中请通过PubMed、Web of Science等数据库检索真实文献。*
**Background of Recombinant PGF Protein**
Placental Growth Factor (PGF), a member of the vascular endothelial growth factor (VEGF) family, plays a critical role in angiogenesis and vascular remodeling. Initially identified for its expression in placental tissues during embryogenesis, PGF binds to VEGF receptor-1 (VEGFR-1) and neuropilin co-receptors, modulating endothelial cell proliferation, migration, and survival. Unlike VEGF-A, which is essential for developmental and pathological angiogenesis, PGF primarily amplifies angiogenic signaling under ischemic or inflammatory conditions, making it a key mediator in diseases like cancer, diabetic retinopathy, and cardiovascular disorders.
Recombinant PGF protein is engineered using genetic modification techniques, often expressed in mammalian cell systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications. This bioengineered form retains the functional specificity of native PGF, enabling researchers to study its mechanisms in vitro and in vivo. Its applications span basic research—such as elucidating angiogenic pathways—and therapeutic development, including anti-angiogenic therapies or tissue regeneration strategies.
Recent studies highlight PGF's dual role: while it promotes pathological angiogenesis in tumors, it also supports vascular repair in ischemic tissues. Such duality has spurred interest in developing PGF-targeted therapies, including neutralizing antibodies or recombinant PGF as a potential treatment for vascular insufficiency. Additionally, recombinant PGF serves as a critical reagent in diagnostic assays to quantify PGF levels in clinical samples, aiding disease prognosis and monitoring.
Overall, recombinant PGF protein remains a vital tool for advancing both mechanistic understanding and clinical innovation in angiogenesis-related diseases.
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