H9786
Anti-Hepatocyte Growth Factor Receptor (c-Met) antibody produced in goat
affinity isolated antibody, lyophilized powder
Sinônimo(s):
Anti-HGF Receptor
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About This Item
fonte biológica
goat
Nível de qualidade
conjugado
unconjugated
forma do anticorpo
affinity isolated antibody
tipo de produto de anticorpo
primary antibodies
clone
polyclonal
forma
lyophilized powder
reatividade de espécies
human
técnica(s)
flow cytometry: suitable
immunohistochemistry: 5-15 μg/mL
western blot: 0.1-0.2 μg/mL
Impurezas
endotoxin, tested
nº de adesão UniProt
temperatura de armazenamento
−20°C
modificação pós-traducional do alvo
unmodified
Informações sobre genes
human ... MET(4233)
mouse ... Met(17295)
Categorias relacionadas
Descrição geral
The antibody neutralizes receptor-ligand interaction. At 0.5-2 μg/mL the antibody will block 50% of the binding of 5 ng/mL recombinant human HGF to 0.1 μg immobilized recombinant human HGF R/c-MET Fc chimera. >90% of the binding will be blocked by 10 μg/mL of the antibody.
Imunogênio
purified recombinant human hepatocyte growth factor receptor extracellular domain expressed in mouse NSO cells.
Aplicação
Anti-Hepatocyte Growth Factor Receptor (c-Met) antibody produced in goat was used to block c-Met in HeLa cells.
Ações bioquímicas/fisiológicas
Hepatocyte Growth Factor (HGF) is a multifunctional, heparin-binding factor that stimulates the proliferation of liver cells. The cellular effects of HGF are mediated by its receptor, c-Met, that leads to significant activation of ERK, Src/FAK, STAT3 and PI3K signaling. Various functions of the HGF/c-Met signaling include proliferation, cell survival, motility and adhesion and tissue regeneration. Apart from liver, HGF also mediates regeneration of kidney, lung and gastro-intestines.
forma física
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing carbohydrates.
Exoneração de responsabilidade
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
Certificados de análise (COA)
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Peter J Ansell et al.
European journal of cancer (Oxford, England : 1990), 46(5), 966-973 (2010-01-12)
The blood protein plasminogen is proteolytically cleaved to produce angiostatin and kringle 5 (K5), both of which are known angiogenesis inhibitors. A common structural element between K5, angiostatin and other endogenous angiogenesis inhibitors is the presence of the kringle protein-interacting
Silvia Goldoni et al.
The Journal of cell biology, 185(4), 743-754 (2009-05-13)
Decorin, a member of the small leucine-rich proteoglycan gene family, impedes tumor cell growth by down-regulating the epidermal growth factor receptor. Decorin has a complex binding repertoire, thus, we predicted that decorin would modulate the bioactivity of other tyrosine kinase
Simone Buraschi et al.
The Journal of biological chemistry, 285(53), 42075-42085 (2010-10-27)
A theme emerging during the past few years is that members of the small leucine-rich proteoglycan gene family affect cell growth by interacting with multiple receptor tyrosine kinases (RTKs), mostly by a physical down-regulation of the receptors, thereby depriving tumor
Shinya Mizuno et al.
Frontiers in bioscience : a journal and virtual library, 13, 7072-7086 (2008-05-30)
Hepatocyte growth factor (HGF) and Met/HGF receptor play roles in dynamic growth and morphogenesis during development and regeneration of organs, including the kidney. In the kidney, HGF targets different types of cells, while its biological actions depend on a target
Weon-Kyoo You et al.
BMB reports, 41(12), 833-839 (2009-01-07)
Angiogenesis in tumors is driven by multiple growth factors that activate receptor tyrosine kinases. An important driving force of angiogenesis in solid tumors is signaling through vascular endothelial growth factor (VEGF) and its receptors (VEGFRs). Angiogenesis inhibitors that target this
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