|HGF R/c‑MET in HT‑29 and U937 Human Cell Lines. HGF R/c‑MET was detected in immersion fixed HT‑29 human colon adenocarcinoma cell line (left panel) and U937 human histiocytic lymphoma cell line (right panel) using Goat Anti-Mouse HGF R/c‑MET Antigen Affinity-purified Polyclonal Antibody (Catalog # AF527) at 5 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). Specific staining was localized to plasma membrane. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
|HGF R/c‑MET in Mouse Embryo. HGF R/c‑MET was detected in immersion fixed frozen sections of mouse embryo (15 d.p.c.) using Goat Anti-Mouse HGF R/c‑MET Antigen Affinity-purified Polyclonal Antibody (Catalog # AF527) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm in muscle cells. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.|
HGF R, also known as Met (from N-methyl-N’-nitro-N-nitrosoguanidine induced), is a glycosylated receptor tyrosine kinase that plays a central role in epithelial morphogenesis and cancer development. HGF R is synthesized as a single chain precursor which undergoes cotranslational proteolytic cleavage. This generates a mature HGF R that is a disulfide-linked dimer composed of a 50 kDa extracellular alpha chain and a 145 kDa transmembrane beta chain (1, 2). The extracellular domain (ECD) contains a seven bladed beta -propeller sema domain, a cysteine-rich PSI/MRS, and four Ig-like E-set domains, while the cytoplasmic region includes the tyrosine kinase domain (3, 4). An alternately spliced form of mouse HGF R lacks a cytoplasmic juxtamembrane region important for regulation of signal transduction (5, 6). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 7). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (8, 9). HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation (10). In the absence of ligand, HGF R forms non-covalent complexes with a variety of membrane proteins including CD44v6, CD151, EGF R, Fas, integrin alpha 6/ beta 4, plexins B1, 2, 3, and MSP R/Ron (11-18). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (11-18). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (11, 15, 16). Paracrine induction of epithelial cell scattering and branching tubulogenesis results from the stimulation of HGF R on undifferentiated epithelium by HGF released from neighboring mesenchymal cells (19). Genetic polymorphisms, chromosomal translocation,
over-expression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, mouse HGF R shares 87%, 87%, and 94% amino acid sequence identity with canine, human, and rat HGF R, respectively.
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