PLGF1 Human, Sf9
Description
Production and Purification
PLGF1 Human, Sf9 is generated using baculovirus expression in Sf9 cells. Critical steps include:
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Vector Design: Codon-optimized PLGF1 gene cloned into baculovirus transfer plasmids .
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Cell Line Engineering: Stable Sf9 cell lines with caspase-1 suppression to enhance yield by delaying apoptosis .
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Purification: Proprietary chromatography (e.g., affinity tags like His-tag) achieves >95% purity .
Yield Optimization:
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Caspase-1-repressed Sf9 cells increase recombinant protein production by 1.5–2.5× compared to wild-type cells .
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Chaperone proteins (e.g., HSC70, HSP90) show upregulated expression during infection, aiding protein folding .
Functional Role and Receptor Interaction
PLGF1 binds exclusively to VEGFR-1 (Flt-1) via key residues mapped through structural studies :
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Binding Interface: Hydrophobic residues (Leu-38, Phe-40) and polar residues (Arg-43, Glu-67) mediate Flt-1 interaction .
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Biological Effects:
Diagnostic Use
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Pre-eclampsia Biomarker: PLGF1 levels correlate with placental insufficiency; commercial ELISA kits use recombinant PLGF1 for quantification .
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Cardiovascular Disease: Elevated PLGF1 predicts adverse outcomes in heart failure (NYHA Class III/IV) .
Therapeutic Development
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Chimeric Constructs: Fusion proteins (e.g., VEGF-ENZ7/PlGF) reduce immunogenicity while retaining receptor specificity .
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Antibody Production: Monoclonal antibodies against PLGF1 (e.g., SEQ ID NO:32) enable targeted inhibition of pathological angiogenesis .
Comparative Expression Data
Recombinant PLGF1 production in Sf9 cells vs. mammalian systems:
Product Specs
PIGF, PGF, PLGF-1.
Product Science Overview
Placental Growth Factor-1 (PLGF-1) is a member of the vascular endothelial growth factor (VEGF) family, which plays a crucial role in angiogenesis and vasculogenesis. This protein is particularly significant in the context of pregnancy, where it contributes to the development of the placenta and the establishment of a healthy blood supply to the fetus.
PLGF-1 is a glycosylated polypeptide chain that forms a homodimer. The human recombinant version of PLGF-1 produced in Sf9 insect cells consists of two polypeptide chains, each containing 131 amino acids, resulting in a total molecular mass of approximately 34 kDa . The recombinant protein is purified using proprietary chromatographic techniques to ensure high purity and activity .
PLGF-1 is primarily involved in the regulation of angiogenesis, the process by which new blood vessels form from pre-existing vessels. This is essential for the proper development of the placenta during pregnancy. PLGF-1 binds to the VEGF receptor-1 (VEGFR-1), promoting endothelial cell proliferation, migration, and survival. It also enhances the permeability of blood vessels, facilitating the exchange of nutrients and waste products between the mother and the fetus.
PLGF-1 has been extensively studied for its role in various pathological conditions, particularly in pregnancy-related disorders such as pre-eclampsia. Pre-eclampsia is characterized by high blood pressure and proteinuria, and it can lead to serious complications for both the mother and the baby if not properly managed. PLGF-based diagnostic tests are used to help diagnose and monitor pre-eclampsia, providing valuable information for clinical decision-making .
The recombinant form of PLGF-1 is widely used in research to study its biological functions and potential therapeutic applications. It is also used in the development of diagnostic assays for pre-eclampsia and other conditions associated with abnormal angiogenesis. The availability of high-quality recombinant PLGF-1 allows researchers to conduct detailed studies on its mechanisms of action and interactions with other proteins.
