Home / PlGF-2 / Recombinant Mouse PlGF-2 Protein

Recombinant Mouse PlGF-2 Protein

Catalog #: 465-PL
11 Citations Datasheet / COA / SDS

Carrier Free

Catalog # Availability Size / Price Qty
465-PL-010/CF
465-PL-050/CF

With Carrier

Catalog # Availability Size / Price Qty
465-PL-010
465-PL-050
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Citations (11)
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Mouse PlGF-2 Protein Summary

Product Specifications

Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
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 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
Analysis
Ala24 & Ala27
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
15.1 kDa (monomer)
SDS-PAGE
15-22 kDa, under reducing conditions.

Product Datasheets

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465-PL (with carrier)

Product Datasheet
COA
SDS

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465-PL/CF (carrier free)

Product Datasheet
COA
SDS

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.

465-PL

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
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.

465-PL/CF

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
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.
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-2

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).

References
  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.
Long Name
Placenta Growth Factor 2
Entrez Gene IDs
5228 (Human); 18654 (Mouse)
Alternate Names
OORS; PlGF2; PlGF-2

Citations for Recombinant Mouse PlGF-2 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.

11 Citations: Showing 1 - 10
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  1. Inhibition of FLT1 ameliorates muscular dystrophy phenotype by increased vasculature in a mouse model of Duchenne muscular dystrophy
    Authors: M Verma, Y Shimizu-Mo, Y Asakura, JP Ennen, J Bosco, Z Zhou, GH Fong, S Josiah, D Keefe, A Asakura
    PLoS Genet., 2019-12-26;15(12):e1008468.
    Species: Mouse
    Sample Types:
    Applications: Bioassay
  2. Tumor angiogenesis is differentially regulated by phosphorylation of endothelial cell focal adhesion kinase tyrosines-397 and -861
    Authors: 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
    Cancer Res., 2019-06-12;0(0):.
    Species: Transgenic Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  3. Injured Axons Instruct Schwann Cells to Build Constricting Actin Spheres to Accelerate Axonal Disintegration
    Authors: 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
    Cell Rep, 2019-06-11;27(11):3152-3166.e7.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  4. 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.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  5. Temporal expression of growth factors triggered by epiregulin regulates inflammation development.
    Authors: 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
    J Immunol, 2015-01-02;194(3):1039-46.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  6. NO triggers RGS4 degradation to coordinate angiogenesis and cardiomyocyte growth.
    Authors: Jaba I, Zhuang Z, Li N, Jiang Y, Martin K, Sinusas A, Papademetris X, Simons M, Sessa W, Young L, Tirziu D
    J Clin Invest, 2013-04-01;123(4):1718-31.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Bioassay
  7. 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.
    Species: Mouse
    Sample Types: N/A
    Applications: In Vivo
  8. 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., 2010-03-29;285(22):16713-22.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. VEGF guides angiogenic sprouting utilizing endothelial tip cell filopodia.
    Authors: Gerhardt H, Golding M, Fruttiger M, Ruhrberg C, Lundkvist A, Abramsson A, Jeltsch M, Mitchell C, Alitalo K, Shima D, Betsholtz C
    J. Cell Biol., 2003-06-16;161(6):1163-77.
    Species: Rat
    Sample Types: In Vivo
    Applications: In Vivo
  10. 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., 2003-03-01;111(5):649-58.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  11. 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, 2002-09-05;101(2):560-7.
    Applications: ELISA (Standard)

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