Recombinant Human PlGF Protein

Formulations:
Catalog # Availability Size / Price Qty
264-PGB-010
264-PGB-050
Recombinant Human PlGF Protein Bioactivity
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Product Details
Citations (21)
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Recombinant Human PlGF Protein Summary

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. When Recombinant Human VEGF R1/Flt‑1 Fc Chimera (Catalog # 3516-FL) is immobilized at 0.5 μg/mL, 100 μL/well, the concentration of Recombinant Human PlGF that produces 50% of the optimal binding response is approximately 0.15-0.9 ng/mL.
Source
E. coli-derived human PlGF protein
Ala21-Arg149
Accession #
N-terminal Sequence
Analysis
Ala21
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
15 kDa
SDS-PAGE
12-15 kDa, reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

264-PGB

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Reconstitution Reconstitute at 200 μg/mL in 4 mM HCl.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

264-PGB/CF

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitution Reconstitute at 200 μg/mL in 4 mM HCl.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Data Image

Bioactivity Recombinant Human PlGF Protein Bioactivity View Larger

When Recombinant Human VEGF R1/Flt-1 Fc Chimera, aa 27-328 (Catalog # 3516-FL) is coated at 0.5 µg/mL, Recombinant Human PlGF (Catalog # 264-PGB) binds with a typical ED50 of 0.15-0.9 ng/mL.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: PlGF

Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines (1, 2). Alternative 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, 2). Only PlGF-2 contains a highly basic heparin-binding 21 aa insert at the C-terminus (1). Human PlGF-1 shares 56%, 55%, 74% and 95% aa identity with the comparable isoform of mouse, rat, canine, and equine PlGF, respectively. PlGF is mainly found as variably glycosylated, secreted, 55-60 kDa disulfide linked homodimers (3). Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes, and some endothelial cells (1, 4-6). Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia (7). However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia (8). 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, 4, 8, 9). However, PlGF (especially PlGF-1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2 (3, 4). PlGF-2, but not PLGF-1, shows heparin-dependent binding of Neuropilin (Npn)-1 and Npn-2 (10, 11). PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound, bone fracture, and cardiac repair, but also contribute to inflammation in active sickle cell disease and atherosclerosis (5, 6, 8, 12-15). PlGF can also inhibit TIMP3 expression in the spleen, leading to immune triggering of hypertension (16).

References
  1. Hauser, S. and H.A. Weich (1993) Growth Factors 9:259.
  2. Maglione, D. et al. (1993) Oncogene 8:925.
  3. Eriksson, A. et al. (2002) Cancer Cell 1:99.
  4. Ribatti, D. (2008) Angiogenesis 11:215.
  5. Oura, H. et al. (2003) Blood 101:560.
  6. Roncal, C. et al. (2010) Cardiovasc. Res. 86:29.
  7. Levine, R.J. et al. (2004) N. Engl. J. Med. 350:672.
  8. Carmeliet, P. et al. (2001) Nat. Med. 7:575.
  9. Autiero, M. et al. (2003) Nat. Med. 9:936.
  10. Migdal, M. et al. (1998) J. Biol. Chem. 273:22272.
  11. Cheng, L. et al. (2004) J. Biol. Chem. 279:30654.
  12. Perelman, N. et al. (2003) Blood 102:1506.
  13. Cianfarani, F. et al. (2006) Am. J. Pathol. 169:1167.
  14. Maes, C. et al. (2006) J. Clin. Invest. 116:1230.
  15. Iwasaki, H. et al. (2011) PLoS One 6:e24872.
  16. Carnevale, D. et al. (2014) Immunity 41:737.
Long Name
Placenta Growth Factor
Entrez Gene IDs
5228 (Human); 18654 (Mouse)
Alternate Names
D12S1900; PGF; PGFL; placenta growth factor; placental growth factor; placental growth factor, vascular endothelial growth factor-related protein; PlGF; PlGF-2; PLGFplacental growth factor-like; SHGC-10760

Citations for Recombinant Human PlGF Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

21 Citations: Showing 1 - 10
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  1. MicroRNA 648 Targets ET-1 mRNA and is cotranscriptionally regulated with MICAL3 by PAX5.
    Authors: Li C, Gonsalves C, Eiymo Mwa Mpollo M, Malik P, Tahara S, Kalra V
    Mol Cell Biol, 2015;35(3):514-28.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Interaction of mesenchymal stem cells with fibroblast-like synoviocytes via cadherin-11 promotes angiogenesis by enhanced secretion of placental growth factor.
    Authors: Park, Su-Jung, Kim, Ki-Jo, Kim, Wan-Uk, Cho, Chul-Soo
    J Immunol, 2014;192(7):3003-10.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Elastase induces lung epithelial cell autophagy through placental growth factor: a new insight of emphysema pathogenesis.
    Authors: Hou H, Cheng S, Chung K, Kuo M, Yeh C, Chang B, Lu H, Wang H, Yu C
    Autophagy, 2014;10(9):1509-21.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Characterisation of syncytiotrophoblast vesicles in normal pregnancy and pre-eclampsia: expression of Flt-1 and endoglin.
    Authors: Tannetta D, Dragovic R, Gardiner C, Redman C, Sargent I
    PLoS ONE, 2013;8(2):e56754.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Endorepellin, the angiostatic module of perlecan, interacts with both the alpha2beta1 integrin and vascular endothelial growth factor receptor 2 (VEGFR2): a dual receptor antagonism.
    Authors: Goyal A, Pal N, Concannon M, Paul M, Doran M, Poluzzi C, Sekiguchi K, Whitelock JM, Neill T, Iozzo RV
    J. Biol. Chem., 2011;286(29):25947-62.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Binding Displacement
  6. Placental growth factor neutralising antibodies give limited anti-angiogenic effects in an in vitro organotypic angiogenesis model.
    Authors: Brave SR, Eberlein C, Shibuya M, Wedge SR, Barry ST
    Angiogenesis, 2010;13(4):337-47.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Placenta growth factor (PlGF), a novel inducer of plasminogen activator inhibitor-1 (PAI-1) in sickle cell disease (SCD).
    Authors: Patel N, Sundaram N, Yang M
    J. Biol. Chem., 2010;285(22):16713-22.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. VEGF-A and VEGF-F evoke distinct changes in vascular ultrastructure.
    Authors: Matsunaga Y, Yamazaki Y, Suzuki H, Morita T
    Biochem. Biophys. Res. Commun., 2009;379(4):872-5.
    Species: Guinea Pig
    Sample Types: In Vivo
    Applications: In Vivo
  9. Modulation of angiogenesis by a tetrameric tripeptide that antagonizes vascular endothelial growth factor receptor 1.
    Authors: Ponticelli S, Marasco D, Tarallo V, Albuquerque RJ, Mitola S, Takeda A, Stassen JM, Presta M, Ambati J, Ruvo M, De Falco S
    J. Biol. Chem., 2008;283(49):34250-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  10. Placental growth factor down-regulates type 1 T helper immune response by modulating the function of dendritic cells.
    Authors: Lin YL, Liang YC, Chiang BL
    J. Leukoc. Biol., 2007;82(6):1473-80.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  11. alpha2beta1 integrin expression in the tumor microenvironment enhances tumor angiogenesis in a tumor cell-specific manner.
    Authors: Zhang Z, Ramirez NE, Yankeelov TE, Li Z, Ford LE, Qi Y, Pozzi A, Zutter MM
    Blood, 2007;111(4):1980-8.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  12. Insulin-like growth factor binding protein-4 (IGFBP-4) is a novel anti-angiogenic and anti-tumorigenic mediator secreted by dibutyryl cyclic AMP (dB-cAMP)-differentiated glioblastoma cells.
    Authors: Moreno MJ, Ball M, Andrade MF, McDermid A, Stanimirovic DB
    Glia, 2006;53(8):845-57.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  13. Loss of SPARC-mediated VEGFR-1 suppression after injury reveals a novel antiangiogenic activity of VEGF-A.
    Authors: Nozaki M, Sakurai E, Raisler BJ, Baffi JZ, Witta J, Ogura Y, Brekken RA, Sage EH, Ambati BK, Ambati J
    J. Clin. Invest., 2006;116(2):422-9.
    Species: Mouse
    Sample Types:
    Applications: In Vivo
  14. Placenta growth factor in diabetic wound healing: altered expression and therapeutic potential.
    Authors: Cianfarani F, Zambruno G, Brogelli L, Sera F, Lacal PM, Pesce M, Capogrossi MC, Failla CM, Napolitano M, Odorisio T
    Am. J. Pathol., 2006;169(4):1167-82.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  15. Inhibition of prostate tumor growth and bone remodeling by the vascular targeting agent VEGF121/rGel.
    Authors: Mohamedali KA, Poblenz AT, Sikes CR, Navone NM, Thorpe PE, Darnay BG, Rosenblum MG
    Cancer Res., 2006;66(22):10919-28.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  16. VEGF receptor 1 signaling is essential for osteoclast development and bone marrow formation in colony-stimulating factor 1-deficient mice.
    Authors: Niida S, Kondo T, Hiratsuka S, Hayashi S, Amizuka N, Noda T, Ikeda K, Shibuya M
    Proc. Natl. Acad. Sci. U.S.A., 2005;102(39):14016-21.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  17. Microvascular patterning is controlled by fine-tuning the Akt signal.
    Authors: Sun JF, Phung T, Shiojima I, Felske T, Upalakalin JN, Feng D, Kornaga T, Dor T, Dvorak AM, Walsh K, Benjamin LE
    Proc. Natl. Acad. Sci. U.S.A., 2005;102(1):128-33.
    Species: Bovine
    Sample Types: Whole Cells
    Applications: Bioassay
  18. Differential roles of vascular endothelial growth factor receptors 1 and 2 in dendritic cell differentiation.
    Authors: Dikov MM, Ohm JE, Ray N, Tchekneva EE, Burlison J, Moghanaki D, Nadaf S, Carbone DP
    J. Immunol., 2005;174(1):215-22.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  19. Impairment in ischemia-induced neovascularization in diabetes: bone marrow mononuclear cell dysfunction and therapeutic potential of placenta growth factor treatment.
    Authors: Tamarat R, Silvestre JS, Le Ricousse-Roussanne S, Barateau V, Lecomte-Raclet L, Clergue M, Duriez M, Tobelem G, Levy BI
    Am. J. Pathol., 2004;164(2):457-66.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  20. Excess placental soluble fms-like tyrosine kinase 1 (sFlt1) may contribute to endothelial dysfunction, hypertension, and proteinuria in preeclampsia.
    Authors: Maynard SE, Min JY, Merchan J, Lim KH, Mondal S, Stillman IE, Epstein FH, Karumanchi SA
    J. Clin. Invest., 2003;111(5):649-58.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  21. A critical role of placental growth factor in the induction of inflammation and edema formation.
    Authors: Oura H, Bertoncini J, Velasco P, Brown LF, Carmeliet P, Detmar M
    Blood, 2002;101(2):560-7.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo

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