详细说明
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.
Activity
Measured by its binding ability in a functional ELISA. When Recombinant Human VEGF R1/Flt‑1 Fc Chimera (Catalog # ) 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 0.15-0.9 ng/mL.
Source
E. coli-derived Ala21-Arg149
Accession #
N-terminal Sequence
AnalysisAla21
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
15 kDa
SDS-PAGE
12-15 kDa, reducing conditions
Carrier Free
What does CF mean?
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.
What formulation is right for me?
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.
264-PGB |
| 264-PGB/CF |
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein. | Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. | |
Reconstitution Reconstitute at 200 μg/mL in 4 mM HCl. | 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. | 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.
| Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Data Images
Bioactivity
| When Recombinant Human VEGF R1/Flt-1 Fc Chimera, aa 27-328 (Catalog # ) is coated at 0.5 µg/mL, Recombinant Human PlGF (Catalog # 264-PGB) binds with a typical ED50 of 0.15-0.9 ng/mL. |
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:
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.
Long Name:
Placenta Growth Factor
Entrez Gene IDs:
5228 (Human); 18654 (Mouse)
Alternate Names:
D12S1900; PGF; PGFL; placenta growth factor; placental growth factor; placental growth factor, vascular endothelial growth factor-related protein; PlGF; PlGF-2; PLGFplacental growth factor-like; SHGC-10760








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