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Merck

H9786

Sigma-Aldrich

Anti-Hepatocyte Growth Factor Receptor (c-Met) antibody produced in goat

affinity isolated antibody, lyophilized powder

Synonym(e):

Anti-HGF Receptor

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

goat

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

lyophilized powder

Speziesreaktivität

human

Methode(n)

flow cytometry: suitable
immunohistochemistry: 5-15 μg/mL
western blot: 0.1-0.2 μg/mL

Verunreinigungen

endotoxin, tested

UniProt-Hinterlegungsnummer

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... MET(4233)
mouse ... Met(17295)

Allgemeine Beschreibung

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.

Immunogen

purified recombinant human hepatocyte growth factor receptor extracellular domain expressed in mouse NSO cells.

Anwendung

Anti-Hepatocyte Growth Factor Receptor (c-Met) antibody produced in goat was used to block c-Met in HeLa cells.

Biochem./physiol. Wirkung

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.

Physikalische Form

Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing carbohydrates.

Haftungsausschluss

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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Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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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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