Human PlGF-1

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Size2 µg
Price90 €
SourceInsect cells
Purity Confirmation> 95% by SDS-PAGE
Length [aa]131
Molecular Weight~34.0 kDa
Biological ActivityMeasured by its ability to bind to immobilized rh-sFlt-1 in a functional ELISA. Recombinant human PlGF-1 can bind to immobilized rh-sFlt-1 (100ng/well) with a linear range at 0.5 - 10ng/ml.
Species ReactivityHuman
Buffer50mM acetic acid
Stabilizer/CarrierBSA (50-fold)
ReconstitutionCentrifuge vial prior to opening. The PlGF-1 is supplied in lyophilized form with carrier-protein (BSA) and can be reconstituted with 50mM acetic acid or PBS/water. This solution can be diluted into other buffered solutions or stored frozen for future use.
Stability and StorageThe lyophilized human PlGF-1, though stable at room temperature, is best stored in working aliquots at -20°C to -70°C. Avoid repeated freeze-thaw cycles.
SynonymsPlGF; placental growth factor
DescriptionHuman 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 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 very related protein of PlGF is VEGF with about 53% homology and VEGF-B with similar biological activities.
Uniprot IDP49763
Protein RefSeqNP_001193941.1
mRNA RefSeqNM_001207012.1



  1. The Anti-Vascular Endothelial Growth Factor Receptor 1 (VEGFR-1) D16F7 Monoclonal Antibody Inhibits Melanoma Adhesion to Soluble VEGFR-1 and Tissue Invasion in Response to Placenta Growth Factor. M. G. Atzori et al., Cancers (Basel). 2022 Nov; 14(22): 5578.
  2. Transforming growth factor‐β1 signalling triggers vascular endothelial growth factor resistance and monocyte dysfunction in type 2 diabetes mellitus. L.‐M. Makowski et al., J Cell Mol Med. 2021 Jun; 25(11): 5316–5325.
  3. Inter-manufacturer Comparison of Automated Immunoassays for the Measurement of Soluble FMS-like Tyrosine kinase-1 and Placental Growth Factor. Y. Kwun Yue Cheng et al., Pregnancy Hypertens. 2019 Jul;17:165-171.
  4. Cryopreservation of primary human monocytes does not negatively affect their functionality or their ability to be labelled with radionuclides: basis for molecular imaging and cell therapy. E. Pardali et al., EJNMMI Res. 2016; 6: 77.
  5. Proteolytic Processing Regulates Placental Growth Factor Activities. D. C. Hoffmann et al., J Biol Chem. 2013 Jun 21; 288(25): 17976–17989.
  6. Autocrine activity of soluble Flt-1 controls endothelial cell function and angiogenesis. S. Ahmad et al., Vasc Cell. 2011; 3: 15.
  7. The VEGF-induced transcriptional response comprises gene clusters at the crossroad of angiogenesis and inflammation. B. Schweighofer et al., Thromb Haemost. 2009 Sep; 102(3): 544–554.

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