An economically priced, mammalian-expressed Version Available!
Details of Functionality
Measured by its ability to induce IL-11 secretion by Saos‑2 human osteosarcoma cells. Hjertner, O. et al. (1999) Blood 94:3883. The ED50 for this effect is 0.1‑0.5 ng/mL. The specific activity of Recombinant Human HGF is approximately 1.5 x 103 IU/μg, which is calibrated against Recombinant Human HGF WHO International Standard (NIBSC code: 96/564).
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human HGF protein Gln32-Ser728 (Asp384Asn, Asp416Asn, Leu622Ser, His645Arg, Val678Ile)
alpha chain: No results obtained; Gln32 predicted beta chain: Val495
Structure / Form
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<1.0 EU per 1 μg of the protein by the LAL method.
53.7 kDa ( alpha chain), 26 kDa ( beta chain). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
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 (1‑5). 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 (6, 7). HGF-dependent c-MET activation is implicated in the development of many human cancers (8). HGF regulates epithelial morphogenesis by inducing cell scattering and branching tubulogenesis (9, 10). HGF induces the up‑regulation of integrin alpha 2 beta 1 in epithelial cells by a selective increase in alpha 2 gene transcription (11). This integrin serves as a collagen I receptor, and its blockade disrupts epithelial cell branching tubulogenesis (11, 12). HGF can also alter epithelium morphology by the induction of nectin‑1 alpha ectodomain shedding, an adhesion protein component of adherens junctions (13). In the thyroid, HGF induces the proliferation, motility, and loss of differentiation markers of thyrocytes and inhibits TSH‑stimulated iodine uptake (14). HGF promotes the motility of cardiac stem cells in damaged myocardium (15).
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We have publications tested in 9 confirmed species: Human, Mouse, Rat, Equine, Fish - Prionace glauca (Blue Shark), Hamster, Porcine, Primate - Macaca fascicularis (Crab-eating Monkey or Cynomolgus Macaque), Squirrel.
We have publications tested in 7 applications: Activation, Bioassay, Cell Culture, Control, ELISA (Standard), In Vivo, Scaffold Fabrication.
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Fish - Prionace glauca (Blue Shark)
Primate - Macaca fascicularis (Crab-eating Monkey or Cynomolgus Macaque)
VEGFR-2 - A highly active kinase VEGFR-2 is a family member of the vascular endothelial growth factor (VEGF) family of membrane receptor tyrosine kinases. It is a key regulator of the process of angiogenesis that takes place during fundamental developmental processes such as embry... Read full blog post.
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