human PlGF-1/His protein Human 2 µg

Human Placenta Growth Factor-1 (PlGF-1), a 19 kDa protein consisting of 131 amino acid residues and fused to a C-terminal His-tag (6x His), 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 controversal. In several reports it was shown not to be a potent mitogen for endotehlial 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 much related protein of PlGF is VEGF with about 53% homology and VEGF-B with similar biological activities.