1. Recombinant Proteins
  2. Cytokines and Growth Factors Receptor Proteins
  3. HGF & Receptors Enzyme-linked receptors
  4. HGF (MET) family

c-Met is a receptor tyrosine kinase encoded for by the c-met proto-oncogene. The c-Met receptor is expressed on the surfaces of various cells. Structurally, c-Met is formed by proteolytic processing of a common precursor in the post-Golgi compartment into a single-pass, disulphide-linked α/β heterodimer. The extracellular portion of c-MET is composed of three domain types, a semaphorin domain (SEMA), which encompasses the whole α-subunit and part of the β-subunit, the PSI domain (found in plexins, semaphorins and integrins), which is connected to the transmembrane helix via four immunoglobulin-plexin-transcription (IPT) domains. Intracellularly, the c-MET receptor contains a tyrosine kinase catalytic domain flanked by distinctive juxtamembrane and carboxy-terminal sequences. c-Met can be activated by its cognate ligand-hepatocyte growth factor (HGF). When the tyrosines within the multifunctional docking site become phosphorylated they recruit signaling effectors, including the adaptor proteins growth factor receptor-bound protein 2 (GRB2), src homology 2 domain-containing (SHC), v-crk sarcoma virus CT10 oncogene homolog (CRK) and CRK-like (CRKL); the effector molecules phosphatidylinositol 3-kinase (PI3K), phospholipase Cγ (PLCγ) and SRC, the src homology 2 domain-containing 5' inositol phosphatase SHIP-2, and the signal transducer and activator of transcription STAT3. These cellular signaling pathways are involved in proliferation, motility, migration and invasion. Therefore, C-MET receptor plays essential roles in controlling a number of critical cellular processes such as cell proliferation, survival, motility, and morphogenesis. (Targeting c-Met/HGFR )

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