Canine c-MET / HGFR Protein (His Tag)
c-Met
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| Catalog Number | P70008-D08H |
|---|---|
| Organism Species | Canine |
| Host | Human Cells |
| Synonyms | c-Met |
| Molecular Weight | The recombinant canine c-Met is a disulfide-linked heterodimer composed of proteolytically cleaved α and β subunits. Each α and β subunit together consists of 922 amino acids and has a predicted molecular mass of 103 (α =33 + β =70) kDa. As a result of glycosylation, the apparent molecular mass of the canine c-Met is approximately 42-47 kDa and 85-95 kDa respectively in SDS-PAGE under reducing conditions. |
| predicted N | Glu 25 |
| SDS-PAGE |  |
| Purity | > 95 % as determined by SDS-PAGE |
| Protein Construction | A DNA sequence encoding the extracellular domain of canine MET (NP_001002963.1) (Met 1-Leu 935) was expressed, with a polyhistidine tag at the N-terminus. |
| Bio-activity | 1. Measured by its binding ability in a functional ELISA. 2. Immobilized human HGF (P10463-HNAS) at 10 μg/mL (100 μl/well) can bind canine c-MET (P70008-D08H), The EC50 of canine c-MET (P70008-D08H) is 7 ng/mL. 3. Immobilized canine MET-His at 10 μg/ml (100 μl/well) can bind biotinylated human HGF-His (P10463-H08H), The EC50 of biotinylated human HGF-His (P10463-H08H) is 0.11-0.25 μg/ml. |
| Research Area | Cancer |Signal transduction |Protein Phosphorylation |Tyrosine Kinase |Receptor Tyrosine Kinases |
| Formulation | Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | Hepatocyte growth factor receptor (HGFR), also known as c-Met or mesenchymal-epithelial transition factor (MET), is a receptor tyrosine kinase (RTK) that has been shown to be overexpressed and/or mutated in a variety of malignancies. HGFR protein is produced as a single-chain precursor, and HGF is the only known ligand. Normal HGF/HGFR signaling is essential for embryonic development, tissue repair or wound healing, whereas aberrantly active HGFR has been strongly implicated in tumorigenesis, particularly in the development of invasive and metastatic phenotypes. HGFR protein is a multifaceted regulator of growth, motility, and invasion, and is normally expressed by cells of epithelial origin. Preclinical studies suggest that targeting aberrant HGFR signaling could be an attractive therapy in cancer. |
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