Recombinant Human PlGF-4 Protein Summary
Product Specifications
Leu19-Arg242
Analysis
Product Datasheets
Carrier Free
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.
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.
8987-PL
| Formulation | Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 250 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.
|
8987-PL/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in HCl. |
| Reconstitution | Reconstitute at 250 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.
|
Reconstitution Calculator
Background: PlGF-4
Placenta growth factor (PlGF or PGF) is an approximately 55-60 kDa member of the PDGF/VEGF family of secreted growth factors that share a conserved pattern of eight cysteines (1). Alternative splicing generates multiple human PlGF isoforms containing 131 (PlGF‑1), 152 (PlGF‑2), 203 (PlGF‑3), or 224 (PlGF-4) amino acids (aa) (2, 3). Mature human PlGF shares 66% and 63% aa sequence identity with comparable regions of mouse and rat PlGF, respectively. PlGF is expressed as a variably glycosylated disulfide linked homodimer by villous trophoblasts and decidual cells, with smaller amounts in erythroblasts, keratinocytes and some endothelial cells
(3-6). Circulating PlGF increases during pregnancy, reaching a peak in mid‑gestation; this increase is attenuated in preeclampsia (7). Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia (8). PlGF binds and signals through VEGF R1/Flt‑1 and Neuropilins (some isoforms), but not VEGF R2/Flk‑1/KDR (8-10). In contrast, VEGF binds both VEGF R1 and R2, but signals mainly 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 (8, 9). However, PlGF (especially PlGF‑1) and some forms of VEGF can form heterodimers that alter the angiogenic effect of VEGF on VEGF R2 (4, 9). PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF (1). These activities facilitate wound and bone fracture healing and also contribute to inflammation in active sickle cell disease and atherosclerosis (1, 5, 6, 8, 11-13).
- Dewerchin, M. and P. Carmeliet (2012) Cold Spring Harb. Perspect. Med. 2:a011056.
- Cao, Y. et al. (1997) Biochem. Biophys. Res. Commun. 253:493.
- Yang, W. et al. (2003) J. Reprod. Immunol. 60:53.
- Eriksson, A. et al. (2002) Cancer Cell 1:99.
- 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.
- 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.
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