Recombinant Mouse PlGF-2 Protein, CF

• Reactivity: Mu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Mouse PlGF-2 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse VEGFR1/Flt-1 Fc Chimera (Catalog # 7756-FL) is immobilized at 2 µg/mL (100 µL/well), Recombinant Mouse PlGF 2 (Catalog # 465-PL) binds with an ED50 of 0.350-3.50 ng/mL.
• Source: Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse PlGF-2 protein Ala24-Pro158 & Ala27-Pro158
• Accession #: Q544A5
• N-terminal Sequence: Ala24 & Ala27
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Pgf
• Purity: >97%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 15.1 kDa (monomer).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 15-22 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
• Purity: >97%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse PlGF-2 Protein, CF

• OORS
• PlGF2
• PlGF-2

Background

Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines (1 - 3). Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF-1), 152 (PlGF-2), and 203 (PlGF-3) amino acids (aa) respectively (1 - 3). Only PlGF-2 contains a highly basic heparin-binding 21 aa insert at the C-terminus (1). In the mouse, only one PlGF that is the equivalent of human PlGF-2 has been identified (3). Mouse PlGF shares 60%, 92%, 62% and 59% aa identity with the appropriate isoform of human, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers (4). Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells (1, 5 - 7). Circulating PlGF increases during human pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia (8). However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia (9). PlGF binds and signals through VEGF R1/Flt-1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2-mediated angiogenesis (1, 5, 9, 10). However, PlGF (especially human PlGF-1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2 (4, 5). PlGF-2, like VEGF 164/165 shows heparin-dependent binding of neuropilin (Npn)-1 and Npn-2 and can inhibit nerve growth cone collapse (11, 12). PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis (6, 7, 9, 13 - 16). Circulating PlGF often correlates with tumor stage and aggressiveness, and therapeutic PlGF antibodies are being investigated to inhibit tumor growth and angiogenesis (5, 13).

1. Hauser, S. and H.A. Weich (1993) Growth Factors 9:259.
2. Maglione, D. et al. (1993) Oncogene 8:925.
3. DiPalma, T. et al. (1996) Mamm. Genome 7:6.
4. Eriksson, A. et al. (2002) Cancer Cell 1:99.
5. Ribatti, D. (2008) Angiogenesis 11:215.
6. Oura, H. et al. (2003) Blood 101:560.
7. Roncal, C. et al. (2010) Cardiovasc. Res. 86:29.
8. Levine, R.J. et al. (2004) N. Engl. J. Med. 350:672.
9. Carmeliet, P. et al. (2001) Nat. Med. 7:575.
10. Autiero, M. et al. (2003) Nat. Med. 9:936.
11. Migdal, M. et al. (1998) J. Biol. Chem. 273:22272.
12. Cheng, L. et al. (2004) J. Biol. Chem. 279:30654.
13. Fischer, C. et al. (2008) Nat. Rev. Cancer 8:942.
14. Perelman, N. et al. (2003) Blood 102:1506.
15. Cianfarani, F. et al. (2006) Am. J. Pathol. 169:1167.
16. Maes, C. et al. (2006) J. Clin. Invest. 116:1230.

Publications for PlGF-2 (465-PL/CF)(11)

Publications using 465-PL/CF

• M Verma, Y Shimizu-Mo, Y Asakura, JP Ennen, J Bosco, Z Zhou, GH Fong, S Josiah, D Keefe, A Asakura Inhibition of FLT1 ameliorates muscular dystrophy phenotype by increased vasculature in a mouse model of Duchenne muscular dystrophy PLoS Genet., 2019-12-26;15(12):e1008468. 2019-12-26 [PMID: 31877123] (Bioassay, Mouse)
• AR Pedrosa, N Bodrug, J Gomez-Escu, EP Carter, LE Reynolds, PN Georgiou, I Fernandez, DM Lees, V Kostourou, AN Alexopoulo, S Batista, B Tavora, B Serrels, M Parsons, T Iskratsch, KM Hodivala-D Tumor angiogenesis is differentially regulated by phosphorylation of endothelial cell focal adhesion kinase tyrosines-397 and -861 Cancer Res., 2019-06-12;0(0):. 2019-06-12 [PMID: 31189647] (In Vivo, Transgenic Mouse)
• A Vaquié, A Sauvain, M Duman, G Nocera, B Egger, F Meyenhofer, L Falquet, L Bartesaghi, R Chrast, CM Lamy, S Bang, SR Lee, NL Jeon, S Ruff, C Jacob Injured Axons Instruct Schwann Cells to Build Constricting Actin Spheres to Accelerate Axonal Disintegration Cell Rep, 2019-06-11;27(11):3152-3166.e7. 2019-06-11 [PMID: 31189102] (Bioassay, Rat)
• The Combination of PlGF Inhibition and MMC as a Novel Anti-Scarring Strategy for Glaucoma Filtration Surgery Invest Ophthalmol Vis Sci, 2016-08-01;57(10):4347-55. 2016-08-01 [PMID: 27556218] (In Vivo, Mouse)
• Harada M, Kamimura D, Arima Y, Kohsaka H, Nakatsuji Y, Nishida M, Atsumi T, Meng J, Bando H, Singh R, Sabharwal L, Jiang J, Kumai N, Miyasaka N, Sakoda S, Yamauchi-Takihara K, Ogura H, Hirano T, Murakami M Temporal expression of growth factors triggered by epiregulin regulates inflammation development. J Immunol, 2015-01-02;194(3):1039-46. 2015-01-02 [PMID: 25556244] (Bioassay, Mouse)
• Jaba I, Zhuang Z, Li N, Jiang Y, Martin K, Sinusas A, Papademetris X, Simons M, Sessa W, Young L, Tirziu D NO triggers RGS4 degradation to coordinate angiogenesis and cardiomyocyte growth. J Clin Invest, 2013-04-01;123(4):1718-31. 2013-04-01 [PMID: 23454748] (Bioassay, Mouse)
• VEGFR1 stimulates a CXCR4-dependent translocation of megakaryocytes to the vascular niche, enhancing platelet production in mice. Blood, 2012-05-31;120(14):2787-95. 2012-05-31 [PMID: 22653973] (In Vivo, Mouse)
• Patel N, Sundaram N, Yang M Placenta growth factor (PlGF), a novel inducer of plasminogen activator inhibitor-1 (PAI-1) in sickle cell disease (SCD). J. Biol. Chem., 2010-03-29;285(22):16713-22. 2010-03-29 [PMID: 20351105] (Bioassay, Human)
• Gerhardt H, Golding M, Fruttiger M, Ruhrberg C, Lundkvist A, Abramsson A, Jeltsch M, Mitchell C, Alitalo K, Shima D, Betsholtz C VEGF guides angiogenic sprouting utilizing endothelial tip cell filopodia. J. Cell Biol., 2003-06-16;161(6):1163-77. 2003-06-16 [PMID: 12810700] (In Vivo, Rat)
• Maynard SE, Min JY, Merchan J, Lim KH, Mondal S, Stillman IE, Epstein FH, Karumanchi SA Excess placental soluble fms-like tyrosine kinase 1 (sFlt1) may contribute to endothelial dysfunction, hypertension, and proteinuria in preeclampsia. J. Clin. Invest., 2003-03-01;111(5):649-58. 2003-03-01 [PMID: 12618519] (Bioassay, Rat)
• Oura H, Bertoncini J, Velasco P, Brown LF, Carmeliet P, Detmar M A critical role of placental growth factor in the induction of inflammation and edema formation. Blood, 2002-09-05;101(2):560-7. 2002-09-05 [PMID: 12393422] (ELISA (Standard))

Bioinformatics

• Gene Symbol: Pgf
• Uniprot:
  • Q544A5()