The mature form of recombinant human c-Met is a disulfide-linked heterodimer composed of proteolytically cleaved α and β subunits. Each α and β subunit together consists of 919 amino acids and has a predicted molecular mass of 103 (α=33 +β=70) kDa. As a result of glycosylation, rh c-MET heterodimer thus migrates with apparent molecular mass of approximately 45 kDa and 85 kDa respectively in SDS-PAGE under reducing conditions.
Lyophilized from sterile 20mM Tris, 150mM NaCl, pH8.5 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
c-MET Protein, Human, Recombinant (ECD, His Tag): Images
Measured by its binding ability in a functional ELISA. Immobilized recombinant human HGF at 10 μg/ml (100 μl/well) can bind biotinylated c-Met. The EC50 of biotinylated c-Met is 5.28 μg/ml.
c-MET Protein, Human, Recombinant (ECD, His Tag): Synonyms
Hepatocyte growth factor receptor (HGFR), also known as c-Met or mesenchymal-epithelial transition factor (MET), is a receptor tyrosine kinase (RTK) that is 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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