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Human PlGF-2

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Cat-Nr.300-020
Size20 µg
Price420 €
SourceInsect cells
Formulationlyophilized
Purity Confirmation> 95% by SDS-PAGE
Length [aa]152
Molecular Weight~45.0 kDa
Biological ActivityMeasured by its ability to bind to immobilized rh-sFlt-1 in a functional ELISA. Recombinant human PlGF-2 can bind to immobilized rh-sFlt-1 (100 ng/well) with a linear range at 0.5 - 10 ng/mL.
Species ReactivityHuman
Buffer50mM acetic acid
Stabilizer/CarrierBSA (50-fold)
ReconstitutionCentrifuge vial prior to opening. The PlGF-2 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 PIGF-2, though stable at room temperature, is best stored in working aliquots at -20°C to -70°C
SynonymsPlGF; placental growth factor
DescriptionHuman Placenta Growth Factor-2 (PlGF-2), a 22 kDa protein consisting of 152 amino acid residues is produced as a homodimer. 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 acts only as a weak mitogen for those cell types possessing receptors for binding (e.g. vascular endothelial cells). 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). In addition to its action as a weak mitogen it is also a chemoattractant for monocytes and endothelial cells. Two different proteins are 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 is apparently a homodimer, but preparations of PlGF show some heterogeneity on SDS gels depending of the varying degrees of glycosylation. All dimeric forms possess similar biological activities. If PlGF is angiogenic in vivo is not clear. However, heterodimers between VEGF and PlGF are mitogenic for endothelial cells and have strong angiogenic activity in vivo (e.g. in the CAM assay or in the cornea pocket assay). 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.
Protein SequenceLPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCRALERLVDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSGDRPSYVELTFSQHVRCECRPLREKMKPERRRPKGRGKRRREKQRPTDCHLCGDAVPRR
Uniprot IDP49763
Protein RefSeqNP_001193941.1
mRNA RefSeqNM_001207012.1

Figures

Figure 1.
SDS-PAGE analysis of recombinant human PlGF-2. Sample was loaded in 15% SDS-polyacrylamide gel under non-reducing conditions and stained with Coomassie blue.
Figure 2.
Functional ELISA: Recombinant human PlGF-2 was coated with 0.5µg/ml and increasing amounts of recombinant human sFlt-1(5) was added as standard [Cat# S01-011]. The monoclonal mouse anti-human VEGFR1/Flt-1 antibody [Cat# 101-M28] in combination with a goat anti-mouse Biotin antibody was used for detection.

Reference

  1. Kir4.2 Potassium Channels in Retinal Pigment Epithelial Cells In Vitro: Contribution to Cell Viability and Proliferation, and Down-Regulation by Vascular Endothelial Growth Factor. M.-C. Beer et al., Biomolecules. 2022 Jun; 12(6): 848.
  2. Osmotic and hypoxic induction of osteopontin in retinal pigment epithelial cells: Involvement of purinergic receptor signaling. M. Hollborn et al., Mol Vis. 2020; 26: 188–203.
  3. Osmotic induction of cyclooxygenase-2 in RPE cells: Stimulation of inflammasome activation. L. Messerschmidt et al., Mol Vis. 2019 Jun 30;25:329-344.
  4. 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.
  5. Activator protein-1 contributes to the NaCl-induced expression of VEGF and PlGF in RPE cells. J. Kleiner et al., Mol Vis. 2018 Oct 9;24:647-666.
  6. Proteolytic Processing Regulates Placental Growth Factor Activities.D. C. Hoffmann et al., J Biol Chem. 2013 Jun 21; 288(25): 17976–17989.
  7. Human blood late outgrowth endothelial cells for gene therapy of cancer: determinants of efficacy. J. Wei et al., Gene Ther. 2007 Feb;14(4):344-56.
  8. Placental growth factor mediates mesenchymal cell development, cartilage turnover, and bone remodeling during fracture repair. C. Maes et al., J Clin Invest. 2006 May 1; 116(5): 1230–1242.
  9. VEGF is a modifier of amyotrophic lateral sclerosis in mice and humans and protects motoneurons against ischemic death. D. Lambrechts et al., Nat Genet. 2003 Aug;34(4):383-94.
  10. Role of PlGF in the intra- and intermolecular cross talk between the VEGF receptors Flt1 and Flk1. M. Autiero et al., Nat Med. 2003 Jul;9(7):936-43.
  11. Revascularization of ischemic tissues by PlGF treatment, and inhibition of tumor angiogenesis, arthritis and atherosclerosis by anti-Flt1. A. Luttun et al., Nat Med. 2002 Aug;8(8):831-40.
  12. Loss of HIF-2alpha and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice. V. Compernolle et al., Nat Med. 2002 Jul;8(7):702-10.
  13. Synergism between vascular endothelial growth factor and placental growth factor contributes to angiogenesis and plasma extravasation in pathological conditions. P. Carmeliet et al., Nat Med. 2001 May;7(5):575-83.
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