Human c-Met/HGFR (His Tag) recombinant protein

Human c-Met/HGFR (His Tag) recombinant protein

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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.

RCCP2; C-MET; AUTS9; HGF; HGFR; MET; AI838057; PAR4

P08581

Human Cells

A DNA sequence encoding the extracellular domain of human c-Met (NP_000236) (Met 1-Thr 932) was fused with a polyhistidine tag at the C-terminus.

Human

The mature form of recombinant human c-Met is a disulfide-linked heterodimer composed of proteolytically cleaved ? and ? subunits. Each ? and ? subunit together consists of 919 amino acids and has a predicted molecular mass of 103 (?=33 +?=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.

> 90 % as determined by SDS-PAGE

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.