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Recombinant Mouse PlGF-2 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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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 #
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.
Publications
Read Publications using
465-PL/CF in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C 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 VEGF164/165, 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.

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

We have publications tested in 4 confirmed species: Human, Mouse, Rat, Transgenic Mouse.

We have publications tested in 3 applications: Bioassay, ELISA (Standard), In Vivo.


Filter By Application
Bioassay
(6)
ELISA (Standard)
(1)
In Vivo
(4)
All Applications
Filter By Species
Human
(1)
Mouse
(5)
Rat
(3)
Transgenic Mouse
(1)
All Species
Showing Publications 1 - 10 of 11. Show All 11 Publications.
Publications using 465-PL/CF Applications Species
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) 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) 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) 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) 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) 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) 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) 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) 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) 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) Bioassay Rat
Show All 11 Publications.

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Bioinformatics

Gene Symbol Pgf
Uniprot