Recombinant Human 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]..
Reference
[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.
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Accession # |
Q07326 |
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Alternate Names |
PlGF; PlGF-2; PLGFplacental growth factor-like; PGFL; placenta growth factor; placental growth factor |
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Source |
Human embryonic kidney cell, HEK293-derived human PIGF protein |
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Protein sequence |
Ala21-Arg149 |
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M.Wt |
14.5 kDa |
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Appearance |
Solution protein |
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Stability & Storage |
Avoid repeated freeze-thaw cycles. It is recommended that hat the protein be aliquoted for optimal storage.- 12 months from date of receipt, -20 to -7°C as supplied. |
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Concentration |
0. 2 mg/mL |
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Formulation |
Dissolved in sterile PBS buffer. |
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Reconstitution |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. This solution can be diluted into other aqueous buffers. |
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Biological Activity |
When Recombinant Human VEGF R1/Flt-1 Fc Chimera 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 0.05-1 ng/ml. Measured by its binding ability in a functional ELISA. |
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Shipping Condition |
Shipping with dry ice. |
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Handling |
Centrifuge the vial prior to opening. |
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Usage |
For Research Use Only! Not to be used in humans. |
Quality Control & DataSheet
- View current batch:
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Purity > 95%, determined by SDS-PAGE.
- Datasheet
Endotoxin: <0.010 EU per 1 ug of the protein by the LAL method.