HGF R/c-MET Antibody (6AT1785) Summary
| Immunogen |
This monoclonal antibody is generated from mice immunized with purified recombinant protein encoding the catalytic domain of human Met.
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| Isotype |
IgG1
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| Clonality |
Monoclonal
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| Host |
Mouse
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| Gene |
MET
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| Purity |
Protein A or G purified
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Applications/Dilutions
| Dilutions |
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Reactivity Notes
This antibody is reactive against Human, Mouse. Please note that this antibody is reactive to Mouse and derived from the same host, Mouse. Additional Mouse on Mouse blocking steps may be required for IHC and ICC experiments. Please contact Technical Support for more information.
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
|
| Buffer |
PBS
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| Preservative |
0.02% Sodium Azide
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| Concentration |
0.25 mg/ml
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| Purity |
Protein A or G purified
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Alternate Names for HGF R/c-MET Antibody (6AT1785)
- AUTS9
- cMET
- c-MET
- EC 2.7.10
- EC 2.7.10.1
- hepatocyte growth factor receptor
- HGF R
- HGF receptor
- HGF/SF receptor
- HGFR
- Met (c-Met)
- met proto-oncogene (hepatocyte growth factor receptor)
- met proto-oncogene tyrosine kinase
- MET
- oncogene MET
- Proto-oncogene c-Met
- RCCP2
- Scatter factor receptor
- SF receptor
- Tyrosine-protein kinase Met
Background
The Met receptor tyrosine kinase is the prototypical member of a small subfamily of growth factor receptors that when activated, induces mitogenic, motogenic, and morphogenic cellular responses. The ligand for Met is hepatocyte growth factor/scatter factor (HGF/SF) and while normal HGF/SF-Met signaling is required for embryonic development, abnormal Met signaling has been strongly implicated in tumorigenesis, particularly in the development of invasive and metastatic phenotypes. Following ligand binding and autophosphorylation, Met transmits intercellular signals using a unique multisubstrate docking site present within the C-terminal end of the receptor. The multisubstrate docking site mediates the binding of several adapter proteins such as Grb2, SHC, Crk/CRKL, and the large adapter protein Gab1. These adapter proteins in turn recruit several signal transducing proteins to form an intricate signaling complex. Analysis of how these adapter proteins bind to the Met receptor and what signal transducers they recruit have led to more substantial models of HGF/SF-Met signal transduction and have uncovered new potential pathways that may be involved into Met mediated tumor cell invasion and metastasis.
