Recombinant Human PlGF Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 264-PGB/CF

R&D Systems, part of Bio-Techne
Catalog #
Availability
Size / Price
Qty
264-PGB-050/CF
264-PGB-010/CF
Print Quote
Bulk Order
Conjugate
Catalog #
Unconjugated
264-PGB
View Product
100% Guarantee

Key Product Details

Source

E. coli

Accession #

NP_001193941.1

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

View all PlGF Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human PlGF protein
Ala21-Arg149

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.

N-terminal Sequence Analysis

Ala21

Predicted Molecular Mass

15 kDa

SDS-PAGE

12-15 kDa, reducing conditions

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 0.75-4.5 ng/mL.

Scientific Data Images for Recombinant Human PlGF Protein, CF

When Recombinant Human VEGF R1/Flt-1 Fc Chimera (3516-FL) is immobilized at 0.5 μg/mL, 100 μL/well, the concentration of Recombinant Human PlGF (Catalog # 264-PGB/CF) that produces 50% of the optimal binding response is approximately 0.75-4.5 ng/mL.

Formulation, Preparation and Storage

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.

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

Alternate Names

PGF, PGFL

Entrez Gene IDs

5228 (Human); 18654 (Mouse)

Gene Symbol

PGF

UniProt

NP_001193941.1

Additional PlGF Products

Product Documents for Recombinant Human PlGF Protein, CF

Product Datasheets

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Download SDS

Product Specific Notices for Recombinant Human PlGF Protein, CF

For research use only

Privacy and Cookie Policy
Site Map
© Copyright 2024 Bio-Techne. All Rights Reserved.