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Recombinant human FGF-b protein

Heparin-Binding Growth Factor 2, Basic Fibroblast Growth Factor
Human Fibroblast Growth Factor-basic, Recombinant, E. coli
Cat #: F-170
Alternative Name Heparin-Binding Growth Factor 2, Basic Fibroblast Growth Factor
Lyophilized Powder yes
  • Bioassay Tested
  • Sterile & Endotoxin Free yes
    Origin Recombinant, E. coli
    MW: 16.5 kDa.
    Endotoxin Level <0.1 EU per 1 µg of the protein by the LAL method.
    Purity: >98% (HPLC)
    Form Lyophilized from a 0.2 µm filtered solution.
    Effective concentration EC50 = ~17 pM.
    Sequence MPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS.
    Structure
    Activity FGF-basic is a heparin binding growth factor which stimulates the proliferation of a wide variety of cells, including mesenchymal, neuroectodermal, endothelial, and smooth muscle cells, among many others. FGF-basic also induces neuronal and glial differentiation, survival and regeneration1-4.
    References-Activity
    1. Burgess, W.H. and Macig, T. (1989) Ann. Rev. Biochem58, 575.
    2. Morrison, R.S. et al. (1986) Proc. Natl. Acad. Sci. U.S.A83, 7537.
    3. Walicke, P. et al. (1986) Proc. Natl. Acad. Sci. U.S.A83, 3012.
    4. Grinspan, J.B. et al. (1993) J. Neurosci. Res36, 672.
    Shipping and storage Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.
    Solubility Sterile water at a concentration of at least 1 µg/0.1 ml.
    BSA (0.1 mg/ml) should be added for more diluted solutions. Centrifuge all product preparations before use (10000 x g 5 min). Repeated freezing/thawing might result in loss of activity.
    Storage of solutions Up to one week at 4°C or four-six weeks at -70°C.
    Our bioassay
    • Alomone Labs Recombinant human FGF-b protein promotes the proliferation of 3T3-L1 cells.
      Alomone Labs Recombinant human FGF-b protein promotes the proliferation of 3T3-L1 cells.
      Cells were cultured with 10% bovine serum for 24 h then the serum was reduced to 0.5% and the cells were stimulated with increasing concentrations of Recombinant human FGF-b protein (#F-170). The cell proliferation was measured 2 days post stimulation using the XTT method.
    References - Scientific background
    1. Ornitz, D.M. and Itoh, N. (2001) Genome Biol. 2, 3005.1.
    2. Fernig, D.G. and Gallagher, J.T. (1994) Prog. Growth Factor Res. 5, 353.
    3. Oda, Y. et al. (2004) J. Oral Maxillofac. Surg. 62, 73.
    4. Yetgin, S. et al. (2001) Leuk. Lymphoma 42, 83.
    5. Strutz, F. et al. (2002) Kidney Int. 61, 1714.
    6. Slavin, J. (1995) Cell Biol. Int. 19, 431.
    7. Bikfalvi, A. et al. (1997) Angiogenesis 1, 155.
    8. Bruno, E. et al. (1991) Blood 77, 2339.
    9. Huang, S. and Terstappen, L.W. (1992) Nature 360, 745.
    10. Bansal, R. and Pfeiffer, S.E. (1997) J. Neurosci. Res. 50, 215.
    11. Halaban, R. (1996) Semin. Oncol. 23, 673.
    12. Florkiewicz, R.Z. and Sommer. A. (1989) Proc. Nat. Acad. Sci. U.S.A. 86, 3978.
    13. Allouche, M. (1995) Leukemia 9, 937.
    14. Mignatti, P. et al. (1992) J. Cell Physiol. 151, 81.
    15. Jaye, M. et al. (1992) Biochim. Biophys. Acta. 1135, 185.
    16. Ornitz, D.M. (2000) BioEssays 22, 108.
    17. Bikfalvi, A. et al. (1997) Endocr. Rev. 18, 26.
    Scientific background

    Fibroblast growth factor-basic (FGF-b, FGF-2) belongs to the 23 member FGF family.1 FGFs play major roles in development,2 wound healing,3 hematopoiesis,4 tumorigenesis,5 and angiogenesis.6 It is expressed mostly in tissues of mesoderm and neuroectoderm origin.7

    FGF-basic exists in four molecular forms, three high molecular weight (21.5, 22, and 24 kDa), and one 18 kDa form.8 The higher molecular weight forms are mainly nucleus associated. The 18 kDa form, which lacks a signal sequence, is cytoplasmic or found at the cell surface.9

    FGF-basic may be released from damaged cells or could be released by an exocytotic mechanism that is independent of the ER-Golgi pathway.10 Secreted FGF interacts with specific cell surface receptors. The FGF receptor family consists of four members: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. These receptors comprise a conserved tyrosine kinase domain, a transmembrane domain and an extracellular ligand binding domain.11 Binding of FGF-basic to its receptor is regulated by heparan sulfate proteoglycans.12

    FGF-basic is implicated in many biological processes. It has been shown to induce endothelial cell proliferation, migration and angiogenesis in vitro and in vivo,13 stimulate myeloid progenitors,14 stimulate stromal growth,15 promote the release of endothelium from its connective tissue anchor (thus encouraging the entry of new vascular endothelium),6 regulate oligodendrocyte progenitor proliferation and differentiation in culture,16 and play a role in the autonomous growth of melanoma cells.17

    Net Peptide Content: 100%
    Last update: 16/08/2020

    Recombinant human FGF-b protein (#F-170) is a highly pure, recombinant, and biologically active protein.

    For research purposes only, not for human use

    Applications

    Specifications

    Scientific Background

    Citations

    Citations
    Product citations
    1. Skalecka, A. et al. (2016) Dev. Neurobiol. 76, 1308.
    2. Brazel, C.Y. et al. (2014) J. Neurochem. 128, 376.
    3. Birenboim, R. et al. (2013) J. Neurosci. Meth. 214, 9.
    4. Liu, X. et al. (2012) Neuropharmacology 62, 901.
    5. Zamburlin P. et al. (2012) Neurosci. Lett. 523, 30.
    6. Ziegler L. et al. (2011) Stem Cell Rev. and Rep7, 394.
    7. Ariano, P. et al. (2006) Cell Calcium 40, 63.
    8. Arriano, P. et al. (2005) J. Neurosci. Meth. 141, 271.
    9. Erriquez, J. et al. (2005) Neurosignals 14, 244.
    10. Vourc’h, P. et al. (2005) Biochem. Biophys. Res. Commun. 332, 215.
    11. Vourc’h, P. et al. (2004) Biochem. Biophys. Res. Commun. 317, 893.
    12. Lobner, D. and Ali, C. (2002) Brain Res. 954, 42.
    13. Romero-Ramos, M. et al. (2002) J. Neurosci. Res. 69, 894.
    14. Tejero-Diez, P. et al. (2000) Mol. Cell. Neurosci. 16, 766.
    15. Charon, I. et al. (1998) Neurochem. Int. 33, 503.
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