Supplier: Biotium

Luteinizing hormone (LH) is a glycoprotein. Each monomeric unit is a sugar-like protein molecule; two of these make the full, functional protein. Its structure is similar to the other glycoproteins, follicle-stimulating hormone (FSH), thyroid-stimulating hormone (TSH), and human chorionic gonadotropin (hCG). The protein dimer contains 2 polypeptide units, labeled alpha and beta subunits that are connected by two bridges. The alpha subunits of LH, FSH, TSH, and hCG are identical, and contain 92 amino acids. The beta subunits vary. LH has a beta subunit of 121 amino acids (LHB) that confers its specific biologic action and is responsible for interaction with the LH receptor. This beta subunit contains the same amino acids in sequence as the beta subunit of hCG and both stimulate the same receptor; however, the hCG beta subunit contains an additional 24 amino acids and the hormones differ in the composition of their sugar moieties.LH is synthesized and secreted by gonadotrophs in the anterior lobe of the pituitary gland. In concert with the other pituitary gonadotropin follicle-stimulating hormone (FSH), it is necessary for proper reproductive function. In the female, an acute rise of LH levels triggers ovulation. In the male, where LH has also been called Interstitial Cell-Stimulating Hormone (ICSH), it stimulates Leydig cell production of testosterone. LH is a useful marker in classification of pituitary tumors and the study of pituitary disease.

Supplier: Biotium

This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.

Supplier: Biotium

This monoclonal antibody is part of a new panel of reagents, which recognizes subcellular organelles or compartments of human cells. These markers may be useful in identification of these organelles in cells, tissues, and biochemical preparations. This MAb recognizes the double stranded DNA in human cells. It can be used to stain the nuclei in cell or tissue preparations and can be used as a nuclear marker in human cells. This MAb produces a homogeneous staining pattern in the nucleus of normal and malignant cells.,Deoxyribonucleic acid (DNA) is a long polymer of nucleotides that is held together by a backbone made of sugars and phosphate groups. It holds the genetic instructions for the development and function of living things. DNA is crucial for living organisms, and all known cellular life and some viruses contain DNA. In eukaryotes, DNA exists in the cell nucleus, while in prokaryotes; DNA is located in the cytoplasm. In living organisms, DNA does not usually exist as a single molecule, but instead as a tightly associated pair of molecules in the shape of a right-handed double helix. Hydrogen bonds as well as forces generated by the hydrophobic effect and pi stacking hold the two DNA strands together. During replication and transcription, portions of the helix unwind and become single stranded. Protective proteins surround these single-stranded DNA. Double stranded (ds) DNA markers are useful tools in biology research and aid in the study of DNA behavior and characteristics.

Supplier: Biotium

This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.

Supplier: Biotium

This monoclonal antibody is part of a new panel of reagents, which recognizes subcellular organelles or compartments of human cells. These markers may be useful in identification of these organelles in cells, tissues, and biochemical preparations. This MAb recognizes the double stranded DNA in human cells. It can be used to stain the nuclei in cell or tissue preparations and can be used as a nuclear marker in human cells. This MAb produces a homogeneous staining pattern in the nucleus of normal and malignant cells.,Deoxyribonucleic acid (DNA) is a long polymer of nucleotides that is held together by a backbone made of sugars and phosphate groups. It holds the genetic instructions for the development and function of living things. DNA is crucial for living organisms, and all known cellular life and some viruses contain DNA. In eukaryotes, DNA exists in the cell nucleus, while in prokaryotes; DNA is located in the cytoplasm. In living organisms, DNA does not usually exist as a single molecule, but instead as a tightly associated pair of molecules in the shape of a right-handed double helix. Hydrogen bonds as well as forces generated by the hydrophobic effect and pi stacking hold the two DNA strands together. During replication and transcription, portions of the helix unwind and become single stranded. Protective proteins surround these single-stranded DNA. Double stranded (ds) DNA markers are useful tools in biology research and aid in the study of DNA behavior and characteristics.

Supplier: Biotium

This monoclonal antibody is part of a new panel of reagents, which recognizes subcellular organelles or compartments of human cells. These markers may be useful in identification of these organelles in cells, tissues, and biochemical preparations. This MAb recognizes the double stranded DNA in human cells. It can be used to stain the nuclei in cell or tissue preparations and can be used as a nuclear marker in human cells. This MAb produces a homogeneous staining pattern in the nucleus of normal and malignant cells.,Deoxyribonucleic acid (DNA) is a long polymer of nucleotides that is held together by a backbone made of sugars and phosphate groups. It holds the genetic instructions for the development and function of living things. DNA is crucial for living organisms, and all known cellular life and some viruses contain DNA. In eukaryotes, DNA exists in the cell nucleus, while in prokaryotes; DNA is located in the cytoplasm. In living organisms, DNA does not usually exist as a single molecule, but instead as a tightly associated pair of molecules in the shape of a right-handed double helix. Hydrogen bonds as well as forces generated by the hydrophobic effect and pi stacking hold the two DNA strands together. During replication and transcription, portions of the helix unwind and become single stranded. Protective proteins surround these single-stranded DNA. Double stranded (ds) DNA markers are useful tools in biology research and aid in the study of DNA behavior and characteristics.

Supplier: Biotium

Glypican-3 (GPC3) is an integral membrane protein that is mutated in the Simpson-Golabi-Behmel syndrome (SGBS). SGBS is characterized by pre- and post-natal overgrowth and is a recessive X-linked condition.GPC3 may also be found in a secreted form. Anti-GPC3 has been identified as a useful tumor marker for the diagnosis of hepatocellular carcinoma (HCC), hepatoblastoma, melanoma, testicular germ cell tumors, and Wilm s tumor. In patients with HCC, GPC3 is overexpressed in neoplastic liver tissue and elevated in serum, but is undetectable in normal liver, benign liver, and the serum of healthy donors. GPC3 expression is also found to be higher in HCC liver tissue than in cirrhotic liver or liver with focal lesions such as dysplastic nodules and areas of hepatic adenoma (HA) with malignant transformation. In the context of testicular germ cell tumors, GPC3 expression is up regulated in certain histologic subtypes, specifically yolk sac tumors and choriocarcinoma. A high level of GPC3 expression has also been found in some types of embryonal tumors, such as Wilm s tumor and hepatoblastoma, with a low or undetectable expression in normal adjacent tissue. In patients with thyroid cancer, expression of GPC3 is dramatically enhanced in certain types of cancers: 100% in follicular carcinoma and 70% in papillary carcinoma. Expression of GPC3 in follicular carcinoma was significantly higher than that of follicular adenoma. In contrast, GPC 3 is not expressed in anaplastic carcinoma.

Supplier: Biotium

Glypican-3 (GPC3) is an integral membrane protein that is mutated in the Simpson-Golabi-Behmel syndrome (SGBS). SGBS is characterized by pre- and post-natal overgrowth and is a recessive X-linked condition.GPC3 may also be found in a secreted form. Anti-GPC3 has been identified as a useful tumor marker for the diagnosis of hepatocellular carcinoma (HCC), hepatoblastoma, melanoma, testicular germ cell tumors, and Wilm s tumor. In patients with HCC, GPC3 is overexpressed in neoplastic liver tissue and elevated in serum, but is undetectable in normal liver, benign liver, and the serum of healthy donors. GPC3 expression is also found to be higher in HCC liver tissue than in cirrhotic liver or liver with focal lesions such as dysplastic nodules and areas of hepatic adenoma (HA) with malignant transformation. In the context of testicular germ cell tumors, GPC3 expression is up regulated in certain histologic subtypes, specifically yolk sac tumors and choriocarcinoma. A high level of GPC3 expression has also been found in some types of embryonal tumors, such as Wilm s tumor and hepatoblastoma, with a low or undetectable expression in normal adjacent tissue. In patients with thyroid cancer, expression of GPC3 is dramatically enhanced in certain types of cancers: 100% in follicular carcinoma and 70% in papillary carcinoma. Expression of GPC3 in follicular carcinoma was significantly higher than that of follicular adenoma. In contrast, GPC 3 is not expressed in anaplastic carcinoma.

Supplier: Biotium

Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI 6.0) subfamilies. This antibody cocktail recognizes acidic (Type I or LMW) and basic (Type II or HMW) cytokeratins, with 67 kDa (CK1); 64 kDa (CK3); 59 kDa (CK4); 58 kDa (CK5); 56 kDa (CK6); 55 kDa (CK7); 52 kDa (CK8); 56.5 kDa (CK10); 53 kDa (CK13); 50 kDa (CK14); 50 kDa (CK15); 48 kDa (CK16); 46 kDa (CK17); 45 kDa (CK18) and 40 kDa (CK19). Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis. KRT-PAN is a broad spectrum anti pan-cytokeratin antibody cocktail, which differentiates epithelial tumors from non-epithelial tumors e.g. squamous vs. adenocarcinoma of the lung, liver carcinoma, breast cancer, and esophageal cancer. It is useful in characterizing the source of various neoplasms and to study the distribution of cytokeratin containing cells in epithelia during normal development and during the development of epithelial neoplasms. This antibody stains cytokeratins present in normal and abnormal human tissues and shows high sensitivity in the recognition of epithelial cells and carcinomas.

Supplier: Biotium

This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.

Supplier: Biotium

This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.

Supplier: Biotium

Luteinizing hormone (LH) is a glycoprotein. Each monomeric unit is a sugar-like protein molecule; two of these make the full, functional protein. Its structure is similar to the other glycoproteins, follicle-stimulating hormone (FSH), thyroid-stimulating hormone (TSH), and human chorionic gonadotropin (hCG). The protein dimer contains 2 polypeptide units, labeled alpha and beta subunits that are connected by two bridges. The alpha subunits of LH, FSH, TSH, and hCG are identical, and contain 92 amino acids. The beta subunits vary. LH has a beta subunit of 121 amino acids (LHB) that confers its specific biologic action and is responsible for interaction with the LH receptor. This beta subunit contains the same amino acids in sequence as the beta subunit of hCG and both stimulate the same receptor; however, the hCG beta subunit contains an additional 24 amino acids and the hormones differ in the composition of their sugar moieties.LH is synthesized and secreted by gonadotrophs in the anterior lobe of the pituitary gland. In concert with the other pituitary gonadotropin follicle-stimulating hormone (FSH), it is necessary for proper reproductive function. In the female, an acute rise of LH levels triggers ovulation. In the male, where LH has also been called Interstitial Cell-Stimulating Hormone (ICSH), it stimulates Leydig cell production of testosterone. LH is a useful marker in classification of pituitary tumors and the study of pituitary disease.

Supplier: Biotium

Luteinizing hormone (LH) is a glycoprotein. Each monomeric unit is a sugar-like protein molecule; two of these make the full, functional protein. Its structure is similar to the other glycoproteins, follicle-stimulating hormone (FSH), thyroid-stimulating hormone (TSH), and human chorionic gonadotropin (hCG). The protein dimer contains 2 polypeptide units, labeled alpha and beta subunits that are connected by two bridges. The alpha subunits of LH, FSH, TSH, and hCG are identical, and contain 92 amino acids. The beta subunits vary. LH has a beta subunit of 121 amino acids (LHB) that confers its specific biologic action and is responsible for interaction with the LH receptor. This beta subunit contains the same amino acids in sequence as the beta subunit of hCG and both stimulate the same receptor; however, the hCG beta subunit contains an additional 24 amino acids and the hormones differ in the composition of their sugar moieties.LH is synthesized and secreted by gonadotrophs in the anterior lobe of the pituitary gland. In concert with the other pituitary gonadotropin follicle-stimulating hormone (FSH), it is necessary for proper reproductive function. In the female, an acute rise of LH levels triggers ovulation. In the male, where LH has also been called Interstitial Cell-Stimulating Hormone (ICSH), it stimulates Leydig cell production of testosterone. LH is a useful marker in classification of pituitary tumors and the study of pituitary disease.

Supplier: Biotium

This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.

Supplier: Biotium

This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.

Supplier: Biotium

Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI 6.0) subfamilies. This antibody cocktail recognizes acidic (Type I or LMW) and basic (Type II or HMW) cytokeratins, with 67 kDa (CK1); 64 kDa (CK3); 59 kDa (CK4); 58 kDa (CK5); 56 kDa (CK6); 55 kDa (CK7); 52 kDa (CK8); 56.5 kDa (CK10); 53 kDa (CK13); 50 kDa (CK14); 50 kDa (CK15); 48 kDa (CK16); 46 kDa (CK17); 45 kDa (CK18) and 40 kDa (CK19). Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis. KRT-PAN is a broad spectrum anti pan-cytokeratin antibody cocktail, which differentiates epithelial tumors from non-epithelial tumors e.g. squamous vs. adenocarcinoma of the lung, liver carcinoma, breast cancer, and esophageal cancer. It is useful in characterizing the source of various neoplasms and to study the distribution of cytokeratin containing cells in epithelia during normal development and during the development of epithelial neoplasms. This antibody stains cytokeratins present in normal and abnormal human tissues and shows high sensitivity in the recognition of epithelial cells and carcinomas.

Supplier: ANTIBODIES.COM

Human CSTF2 ELISA kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human CSTF2 in serum, plasma, tissue homogenates, and other biological fluids.

Supplier: Biotium

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.

Supplier: Biotium

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.

Supplier: Thermo Scientific

SECURITY DEVICE 1 * 1 items

Supplier: Biotium

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.

Supplier: Biotium

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.

Supplier: Biotium

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.

Supplier: Biotium

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.

Supplier: Biotium

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.

Supplier: Biotium

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.

Supplier: Biotium

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.

Supplier: Biotium

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.

Supplier: Biotium

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.

Supplier: Biotium

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.