Placental Growth Factor-3 Human Recombinant
Placental Growth Factor-3 Human Recombinant, sf9
Placental Growth Factor-1 Human Recombinant, Sf9
Placental Growth Factor-2 Human Recombinant
Recombinant Human Placental Growth Factor-2, produced in E. coli, is a homodimer protein that lacks glycosylation. Each polypeptide chain consists of 152 amino acids, linked by disulfide bonds, resulting in a total molecular weight of approximately 34.6kDa.
The purification of PLGF2 is achieved through specific chromatographic techniques developed by the company.
Escherichia Coli.
The product appears as a sterile, white powder that has been lyophilized (freeze-dried) and filtered for sterility.
Placental Growth Factor-2 Human Recombinant, CHO
Placental Growth Factor-2, HEK Human Recombinant
Placental Growth Factor Human Recombinant
Placental Growth Factor Human Recombinant, His Tag
Recombinant human PLGF1, expressed in E. coli bacteria, is a single polypeptide chain consisting of 123 amino acids (a.a 19-131). This non-glycosylated protein includes a 10 amino acid His tag at its N-terminal end. The calculated molecular mass of PLGF1 is 13.8kDa.
Placental Growth Factor-1 Human Recombinant
Placental Growth Factor-1, 132 a.a. Human Recombinant
Recombinant Human Placental Growth Factor-1, produced in E. coli, is a non-glycosylated, disulfide-linked homodimer. Each protein molecule comprises two polypeptide chains, each consisting of 132 amino acids, resulting in a total molecular weight of approximately 29.7kDa. The purification process involves specialized chromatographic techniques.
Escherichia Coli.
Sterile Filtered White lyophilized (freeze-dried) powder.
Placental Growth Factor (PlGF) is a protein encoded by the PGF gene in humans. It belongs to the vascular endothelial growth factor (VEGF) family, which is crucial for angiogenesis and vasculogenesis, particularly during embryogenesis . PlGF is primarily expressed in the placenta but is also found in other tissues .
Key Biological Properties: PlGF is a heparin-binding protein that can form homodimers and heterodimers. It binds to receptors such as FLT1/VEGFR-1 and, in some isoforms, to NRP1/neuropilin-1 and NRP2/neuropilin-2 .
Expression Patterns: PlGF is predominantly expressed in the placental trophoblast during pregnancy. It is also expressed in various tissues, including the renal medulla, cardia, pylorus, and others .
Tissue Distribution: PlGF is found in the placenta, heart, lung, thyroid, liver, skeletal muscle, and bone . Its expression is particularly high in the placenta, where it plays a significant role in fetal development .
Primary Biological Functions: PlGF is involved in angiogenesis, the formation of new blood vessels from pre-existing ones. It promotes the proliferation and migration of endothelial cells . PlGF also plays a role in the recruitment and maturation of bone marrow-derived progenitors involved in the angiogenic process .
Role in Immune Responses and Pathogen Recognition: PlGF has been shown to promote the differentiation and activation of monocyte-macrophage lineage cells, which support the angiogenic stimulus .
Mechanisms with Other Molecules and Cells: PlGF interacts with receptors such as FLT1/VEGFR-1 and NRP1/neuropilin-1. These interactions trigger downstream signaling cascades that promote angiogenesis and endothelial cell growth .
Binding Partners: PlGF binds to FLT1/VEGFR-1 and, in some isoforms, to NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner .
Downstream Signaling Cascades: The binding of PlGF to its receptors activates signaling pathways that lead to the proliferation and migration of endothelial cells, contributing to angiogenesis .
Transcriptional Regulation: The expression of PlGF is regulated at the transcriptional level. Factors such as hypoxia can induce the expression of PlGF .
Post-Translational Modifications: PlGF is secreted as a glycosylated homodimer. Isoforms PlGF-1 and PlGF-3 are diffusible, while PlGF-2 and PlGF-4 have heparin-binding domains and remain cell membrane-associated .
Biomedical Research: PlGF is used in research to understand its role in angiogenesis and its potential therapeutic applications .
Diagnostic Tools: PlGF levels in maternal blood are used to predict and diagnose pre-eclampsia, a pregnancy complication characterized by high blood pressure and damage to other organs .
Therapeutic Strategies: PlGF is being explored as a therapeutic target for conditions such as fetal growth restriction and preeclampsia. Gene therapy approaches are being investigated to enhance PlGF expression and improve placental function .
Development: PlGF plays a crucial role in embryonic development by promoting angiogenesis and vasculogenesis .
Aging and Disease: Dysregulation of PlGF expression is associated with various diseases, including pre-eclampsia and other pregnancy-related complications . PlGF is also being studied for its potential role in cardiovascular diseases and cancer .