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Human PlGF-1
Human PlGF-1
- 中文名称：
- Human PlGF-1
- 英文名称：
- Human PlGF-1
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA79156
- 规格：
- 0.02 mg|2x0.02 mg|3x0.02 mg|4x0.02 mg|5x0.02 mg
- 保存建议：
| Product Form | Temperature | Storage Time |
| Lyophilized | -20°C to -80°C | 1 year |
| Lyophilized | 2°C to 8°C | 6 months |
| Lyophilized | Room Temperature | 1 month |
| Reconstituted | 2°C to 8°C | 1 week |
| Extended Storage | -20°C to -80°C | 3 months |
- 货期：
- 6-8周
- 纯度：
- > 95% by SDS-PAGE & silver stain
- 产品形式：
- Sterile filtered protein solution was lyophilized from 50 mM acetic acid; contains 50x BSA as stabilizer
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 说明书：
Human Placenta Growth Factor-1 (PlGF-1), a 19 kDa protein consisting of 131 amino acid residues is produced as a homodimer. Human Placenta Growth Factor (PlGF) is a polypeptide growth factor and a member of the platelet-derived growth factor family but more related to vascular endothelial growth factor (VEGF). PlGF-1 acts only as a very weak mitogen for some endothelial cell types and as a potent chemoattractant for monocytes. The physiological function in vivo is still controversial. In several reports it was shown not to be a potent mitogen for endothelial cells and not angiogenic in vivo by using different assays. Very recently it was shown by one investigator, that PlGF-1 from cell culture supernatants was angiogenic in the CAM assay and in the rabbit cornea assay. At least one high-affinity receptor for PlGF (FLT-1 or VEGF-R1) has been demonstrated in different primary cell types (e.g. human umbilical vein endothelial cells and monocytes) but PlGF does not bind to KDR/flk-1. Two different proteins can be generated by differential splicing of the human PlGF gene: PlGF-1 (131 aa native chain) and PlGF-2 (152 aa native chain). Both mitogens are secretable proteins, but PlGF-2 can bind to heparin with high affinity. PlGF-1 is a homodimer, but preparations of PlGF show some heterogeneity on SDS gels depending of the varying degrees of glycosylation. All dimeric forms posses a similar biological profile. There is good evidence that heterodimeric molecules between VEGF and PlGF exists and that they are biological active. Different cells and tissues (e.g. placenta) express PlGF-1 and PlGF-2 at different rates. A very related protein of PlGF is VEGF with about 53% homology and VEGF-B with similar biological activities.
