Detection of Recombinant Human HGF by Western Blot. Western blot shows 25 ng of Recombinant Human HGF (Catalog #|
294‑HG), Recombinant Mouse HGF (Catalog # 2207-HG) and Recombinant Canine HGF (Catalog # 3386-HG). PVDF Membrane was probed with 0.1 µg/mL of Goat Anti-Human HGF Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-294-NA) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). Specific bands were detected for HGF at approximately 30 and 60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 3.
HGF in Human Liver. |
HGF was detected in formalin fixed paraffin-embedded sections of human liver using 15 µg/mL Goat Anti-Human HGF Antigen Affinity-purified Polyclonal Antibody (Catalog # AF‑294‑NA) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
IL-11 Secretion Induced by HGF and Neutralization by Human HGF Antibody. |
Recombinant Human HGF induces IL-11 secretion in the Saos‑2 human osteosarcoma cell line. The dose-dependent response (orange line) is measured by the Human IL-11 Duoset (Catalog # DY218). Under these conditions, IL-11 secretion elicited by HGF is neutralized (green line) by increasing concentrations of Goat Anti-Human HGF Antigen Affinity-purified Polyclonal Antibod (Catalog #
HGF, also known as scatter factor and hepatopoietin A, is a pleiotropic protein in the plasminogen subfamily of S1 peptidases. It is a multidomain molecule that includes an N-terminal PAN/APPLE-like domain, four Kringle domains, and a serine proteinase-like domain that has no detectable protease activity. Human HGF is secreted as an inactive 728 amino acid (aa) single chain propeptide. It is cleaved after the fourth Kringle domain by a serine protease to form bioactive disulfide‑linked HGF with a 60 kDa alpha and 30 kDa beta chain. Alternate splicing generates human HGF isoforms that lack the proteinase-like domain and different numbers of the Kringle domains. Human HGF shares 91%‑94% aa sequence identity with bovine, canine, feline, mouse, and rat HGF. HGF binds heparan-sulfate proteoglycans and the widely expressed receptor tyrosine kinase, HGF R/c-MET. HGF-dependent c-MET activation is implicated in the development of many human cancers. HGF regulates epithelial morphogenesis by inducing cell scattering and branching tubulogenesis. HGF induces the upregulation of integrin alpha 2 beta 1 in epithelial cells by a selective increase in alpha 2 gene transcription. This integrin serves as a collagen I receptor, and its blockade disrupts epithelial cell branching tubulogenesis. HGF can also alter epithelium morphology by the induction of nectin-1 alpha ectodomain shedding, an adhesion protein component of adherens junctions. In the thyroid, HGF induces the proliferation, motility, and loss of differentiation markers of thyrocytes and inhibits TSH-stimulated iodine uptake. HGF promotes the motility of cardiac stem cells in damaged myocardium.
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