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 57.8 kDa and 130 kDa respectively in SDS-PAGE under reducing conditions due to glycosylation.
Lyophilized from sterile PBS, 8% Trehalose, pH 7.4 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.
稳定性 & 储存条件
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 & hFc Tag): 图片
Measured by its binding ability in a functional ELISA. Immobilized recombinant human HGF at 1 μg/ml (100μl/well) can bind Human c-MET / HGFR with a linear range of 0.31-160 ng/ml.
c-MET Protein, Human, Recombinant (ECD, His & hFc Tag): 别称
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.