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PLGF, PGFL, PlGF-2, D12S1900, SHGC-10760, placenta growth factor, placental growth factor, vascular endothelial growth factor-related protein, placental growth factor-like |
Description |
Rabbit Anti-Human PGF aa1-20 pAb is produced from sera of rabbits immunized with a highly purified N-terminal peptide of human PGF (placenta growth factor). Anti-PlGF was purified by affinity chromatography with immobilized Protein A. Placenta growth factor (PGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PGF1), 152 (PGF2), and 203 (PGF3) amino acids (aa) respectively. Only PGF2 contains a highly basic heparin binding 21 aa insert at the C-terminus. In the mouse, only one PGF that is the equivalent of human PGF2 has been identified. Human PGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PGF. PGF is mainly found as variably glycosylated, secreted, 55-60 kDa disulfide linked homodimers. Mammalian cells expressing PGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PGF increases during pregnancy, reaching a peak in mid-gestation;, this increase is attenuated in preeclampsia. However, deletion of PGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PGF show impaired angiogenesis in response to ischemia. PGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PGF and VEGF therefore compete for binding to VEGF R1, allowing high PGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PGF (especially PGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PGF2, but not PGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis. |