Recombinant Human PlGF Protein, CF Summary
Details of Functionality |
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. |
Source |
E. coli-derived human PlGF protein Ala21-Arg149 |
Accession # |
|
N-terminal Sequence |
Ala21 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
PGF |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
15 kDa. 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 |
12-15 kDa, reducing conditions |
Publications |
Read Publications using 264-PGB/CF in the following applications:
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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 |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 200 μg/mL in 4 mM HCl. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human PlGF Protein, CF
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, 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).
- Hauser, S. and H.A. Weich (1993) Growth Factors 9:259.
- Maglione, D. et al. (1993) Oncogene 8:925.
- Eriksson, A. et al. (2002) Cancer Cell 1:99.
- Ribatti, D. (2008) Angiogenesis 11:215.
- Oura, H. et al. (2003) Blood 101:560.
- Roncal, C. et al. (2010) Cardiovasc. Res. 86:29.
- Levine, R.J. et al. (2004) N. Engl. J. Med. 350:672.
- Carmeliet, P. et al. (2001) Nat. Med. 7:575.
- Autiero, M. et al. (2003) Nat. Med. 9:936.
- Migdal, M. et al. (1998) J. Biol. Chem. 273:22272.
- Cheng, L. et al. (2004) J. Biol. Chem. 279:30654.
- Perelman, N. et al. (2003) Blood 102:1506.
- Cianfarani, F. et al. (2006) Am. J. Pathol. 169:1167.
- Maes, C. et al. (2006) J. Clin. Invest. 116:1230.
- Iwasaki, H. et al. (2011) PLoS One 6:e24872.
- Carnevale, D. et al. (2014) Immunity 41:737.
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