Recombinant Human PlGF-2 Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human PlGF-2 Protein, CF Summary

• Details of Functionality: Measured in a cell proliferation assay using MDA-MB-231 human breast cancer cells. The ED 50 for this effect is <10 μg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human PlGF-2 protein Leu19-Arg170
• Accession #: NP_002623
• N-terminal Sequence: Leu19
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: PGF
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 17.3 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: 28-33 kDa, 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 HCl.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 200 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human 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). Human PlGF-2 shares 60%, 56%, 82%, 95% and 95% aa identity with mouse, rat, canine, equine and porcine PlGF-2. PlGF is mainly found as a variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimer (4). Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells (1, 5 - 7). Circulating PlGF increases during 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, resulting in a PlGF inhibition of VEGF/VEGF R1 binding coupled to a subsequent promotion of VEGF/VEGF R2-mediated angiogenesis (1, 5, 9, 10). However, PlGF (especially 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, and 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-2 antibodies are being investigated for their ability 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.

Bioinformatics

• Gene Symbol: PGF
• Uniprot:
  • NP_002623(Human)