Human c-MET / HGFR Protein (His & Fc Tag)
AUTS9,c-Met,DFNB97,HGFR,RCCP2
- 100ug (NPP1539) Please inquiry
| Catalog Number | P10692-H03H |
|---|---|
| Organism Species | Human |
| Host | Human Cells |
| Synonyms | AUTS9,c-Met,DFNB97,HGFR,RCCP2 |
| Molecular Weight | The mature recombinant human c-Met/Fc is a disulfide-linked tetramer composed of two proteolytically cleaved α and β subunits. Each α and β together with the C-terminal Fc tag consists of 1155 amino acids and has a predicted molecular mass of 129.5 (α =32.5 + Fc tagged β=97) kDa. The rh c-MET/Fc heterodimer thus migrates with apparent molecular mass of approximately 45 kDa and 120 kDa respectively in SDS-PAGE under reducing conditions due to glycosylation. |
| predicted N | Glu 25 |
| SDS-PAGE |  |
| Purity | > 95 % as determined by SDS-PAGE |
| Protein Construction | A DNA sequence encoding the extracellular domain (Met 1-Thr 932) of human c-Met (NP_000236) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus. |
| Bio-activity | Measured by its binding ability in a functional ELISA. Immobilized recombinant human HGF at 1 μg/ml (100ul/well) can bind Human c-MET / HGFR with a linear range of 0.31-160ng/ml. Scatchard analysis showed the affinity constant (Kd) of human HGF bound to human c-MET / HGFR was 0.52 nM . |
| 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 and mannitol 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. |
| Reference |