Description: Placenta tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl₂, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Description: Working with the fragile RNA molecules requires a great deal of caution, especially when it comes to protecting them from all the RNases that are virtually everywhere. Ensure a successful reverse transcription PCR by protecting you RNAs with our RNase inhibitor.

Description: Human placenta tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human placenta tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated placenta tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated placenta tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.

Description: The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described. These include fibroblast-, platelet derived-, vascular endothelial- and placenta- growth factor (PLGF). Like vascular endothelial growth factor, several PLGF variants have been shown to arise from alternative mRNA splicings. Evidence has suggested VEGF to be an obligatory component in PLGF signaling. While VEGF homodimers and VEGF/PLGF heterodimers function as potent mediators of mitogenic and chemotactic responses in endothelial cells, PLGF homodimers are effectual only at extremely high concentrations. Indeed, many of the physiological effects attributed to VEGF may actually be a result of VEGF/PLGF. VEGF and PLGF share a common receptor, Flt-1, and may also activate Flk-1/KDR.

Description: The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described. These include fibroblast-, platelet derived-, vascular endothelial- and placenta- growth factor (PLGF). Like vascular endothelial growth factor, several PLGF variants have been shown to arise from alternative mRNA splicings. Evidence has suggested VEGF to be an obligatory component in PLGF signaling. While VEGF homodimers and VEGF/PLGF heterodimers function as potent mediators of mitogenic and chemotactic responses in endothelial cells, PLGF homodimers are effectual only at extremely high concentrations. Indeed, many of the physiological effects attributed to VEGF may actually be a result of VEGF/PLGF. VEGF and PLGF share a common receptor, Flt-1, and may also activate Flk-1/KDR.

Description: The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described. These include fibroblast-, platelet derived-, vascular endothelial- and placenta- growth factor (PLGF). Like vascular endothelial growth factor, several PLGF variants have been shown to arise from alternative mRNA splicings. Evidence has suggested VEGF to be an obligatory component in PLGF signaling. While VEGF homodimers and VEGF/PLGF heterodimers function as potent mediators of mitogenic and chemotactic responses in endothelial cells, PLGF homodimers are effectual only at extremely high concentrations. Indeed, many of the physiological effects attributed to VEGF may actually be a result of VEGF/PLGF. VEGF and PLGF share a common receptor, Flt-1, and may also activate Flk-1/KDR.

Description: The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described. These include Fibroblast Growth Factor (FGF), Platelet Derived Growth Factor (PDGF), Vascular Endothelial Growth Factor (VEGF) and Placenta Growth Factor (PLGF). Placenta growth factor (PLGF) is a secreted protein primarily produced by placental trophoblasts but also expressed in other endothelial cells and tumors. There are three isoforms, PLGF-1, PLGF-2, and PLGF-3. PLGF-2 is expressed up until week 8 in the placenta; the placental tissues continuously express PLGF-1 and PLGF-3 but only PLGF-1 is found in colon and mammary carcinomas. PLGF acts to stimulate angiogenesis, endothelial growth and migration. PLGF is a powerful promoter of tumor growth and is upregulated in some cancers, and PLGF is thought to aid in atherosclerotic lesions and neovascular growth surrounding the lesion. Also, PLGF appears to aid aldosterone mediated atherosclerosis. Serum levels of PLGF in some cases are used as a potential biomarker for disease or genetic defect. Recent research indicates that PLGF levels are lower in mothers with Down syndrome fetuses. Evidence has suggested VEGF to be an obligatory component in PLGF signaling. While VEGF homodimers and VEGF/PLGF heterodimers function as potent mediators of mitogenic and chemotactic responses in endothelial cells, PLGF homodimers are effectual only at extremely high concentrations. Indeed, many of the physiological effects attributed to VEGF may actually be a result of VEGF/PLGF. VEGF and PLGF share a common receptor, Flt-1, and may also activate Flk-1/KDR.

Description: The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described. These include Fibroblast Growth Factor (FGF), Platelet Derived Growth Factor (PDGF), Vascular Endothelial Growth Factor (VEGF) and Placenta Growth Factor (PLGF). Placenta growth factor (PLGF) is a secreted protein primarily produced by placental trophoblasts but also expressed in other endothelial cells and tumors. There are three isoforms, PLGF-1, PLGF-2, and PLGF-3. PLGF-2 is expressed up until week 8 in the placenta; the placental tissues continuously express PLGF-1 and PLGF-3 but only PLGF-1 is found in colon and mammary carcinomas. PLGF acts to stimulate angiogenesis, endothelial growth and migration. PLGF is a powerful promoter of tumor growth and is upregulated in some cancers, and PLGF is thought to aid in atherosclerotic lesions and neovascular growth surrounding the lesion. Also, PLGF appears to aid aldosterone mediated atherosclerosis. Serum levels of PLGF in some cases are used as a potential biomarker for disease or genetic defect. Recent research indicates that PLGF levels are lower in mothers with Down syndrome fetuses. Evidence has suggested VEGF to be an obligatory component in PLGF signaling. While VEGF homodimers and VEGF/PLGF heterodimers function as potent mediators of mitogenic and chemotactic responses in endothelial cells, PLGF homodimers are effectual only at extremely high concentrations. Indeed, many of the physiological effects attributed to VEGF may actually be a result of VEGF/PLGF. VEGF and PLGF share a common receptor, Flt-1, and may also activate Flk-1/KDR.

Description: The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described. These include Fibroblast Growth Factor (FGF), Platelet Derived Growth Factor (PDGF), Vascular Endothelial Growth Factor (VEGF) and Placenta Growth Factor (PLGF). Placenta growth factor (PLGF) is a secreted protein primarily produced by placental trophoblasts but also expressed in other endothelial cells and tumors. There are three isoforms, PLGF-1, PLGF-2, and PLGF-3. PLGF-2 is expressed up until week 8 in the placenta; the placental tissues continuously express PLGF-1 and PLGF-3 but only PLGF-1 is found in colon and mammary carcinomas. PLGF acts to stimulate angiogenesis, endothelial growth and migration. PLGF is a powerful promoter of tumor growth and is upregulated in some cancers, and PLGF is thought to aid in atherosclerotic lesions and neovascular growth surrounding the lesion. Also, PLGF appears to aid aldosterone mediated atherosclerosis. Serum levels of PLGF in some cases are used as a potential biomarker for disease or genetic defect. Recent research indicates that PLGF levels are lower in mothers with Down syndrome fetuses. Evidence has suggested VEGF to be an obligatory component in PLGF signaling. While VEGF homodimers and VEGF/PLGF heterodimers function as potent mediators of mitogenic and chemotactic responses in endothelial cells, PLGF homodimers are effectual only at extremely high concentrations. Indeed, many of the physiological effects attributed to VEGF may actually be a result of VEGF/PLGF. VEGF and PLGF share a common receptor, Flt-1, and may also activate Flk-1/KDR.

Description: This cell lysate is prepared from human placenta tissue using Boster's RIPA Lysis Buffer (AR0105) using a standard whole cell lysate protocol. The concentration was determined using the BCA assay process and then diluted using Dithiothreitol (DTT) and a reducing SDS sample loading buffer, heated for 5 minutes at 100˚C.

Description: A Rabbit polyclonal antibody against Human Placenta Growth Factor (PLGF)

Description: A Rabbit polyclonal antibody against Mouse Placenta Growth Factor (PLGF)