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HGF, Human, HEK293 Cells,Tag Free

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HGF, Human, HEK293 Cells,Tag Free: Product Information

  • Purity

    > 95%, determined by SDS-PAGE


  • Endotoxin Level

    <0.010 EU per 1 ug of the protein by the LAL method.


  • Activity

    Measured by its ability to induce IL-11 secretion by Saos-2 human osteosarcoma cells.   

    The EC50 for this effect is 0.05-0.2 ng/mL.


  • Accession #

    P14210


  • Source

    Human embryonic kidney cell, HEK293-derived human HGF protein

    Gln32-Ser728


  • Predicted Moleucular weight

    53.7 kDa ( alpha chain) + 26 kDa ( beta chain)


  • Formulation

    Solution protein

    Dissolved in sterile PBS buffer to a concentration of 0.2 mg/mL.

    This solution can be diluted into other aqueous buffers. Centrifuge the vial prior to opening.


  • Storage and Stability

    Avoid repeated freeze-thaw cycles.

    It is recommended that the protein be aliquoted for optimal storage.

    12 months from date of receipt, -20 to -70 °C as supplied.


  • Shipping

    Shipping with dry ice.


HGF, Human, HEK293 Cells,Tag Free: Product Information

  • 4 ug/lane protein wasresolved with SDS-PAGE undernon-reducing (NR) and reducing (R) conditionsand visualized by CoomassieBlue staining.


  • Size-exclusion chromatography of recombinant human HGF protein (280 nm absorbance) 


  • Recombinant human HGF (Catalog # HF-2008) induces IL11 secretion by Saos-2 human osteosarcoma cells.


HGF, Human, HEK293 Cells,Tag Free: Product Information

  • DFNB39; EC 3.4.21; EC 3.4.21.7; fibroblast-derived tumor cytotoxic factor; F-TCF;HGF; HGFB; HPTA


HGF, Human, HEK293 Cells,Tag Free: Product Information

FHepatocyte Growth Factor (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).


参考文献

1. Karihaloo, A. et al. (2005) Nephron Exp. Nephrol. 100:e40.

2. Hammond, D.E. et al. (2004) Curr. Top. Microbiol. Immunol. 286:21.

3. Rosario, M. and W. Birchmeier (2004) Dev. Cell 7:3.

4. Lesk, A.M. and W.D. Fordham (1996) J. Mol. Biol. 258:501.

5. Nakamura, T. et al. (1989) Nature 342:440.

6. Mizuno, K., et al. (1994) J. Biol. Chem. 269:1131.

7. Gheradi, E. et al. (2003) Proc. Natl. Acad. Sci. 100:12039.

8. Corso, S. et al. (2005) Trends Mol. Med. 11:284.

9. Maeshima, A. et al. (2000) Kid. Int. 58:1511.

10. Montesano, R. et al. (1991) Cell 67:901.

11. Chiu, S-J. et al. (2002) J. Biomed. Sci. 9:261.

12. Saelman, E.U.M. et al. (1995) J. Cell Sci. 108:3531.

13. Tanaka, Y. et al. (2002) Biochem. Biophys. Res. Commun. 299:472.

14. Mineo, R. et al. (1994) Endocrinology 145:4355.

15. Urbanek, K. et al. (2005) Circ. Res. 97:663.


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