Overview
- Burgess, W.H. and Macig, T. (1989) Ann. Rev. Biochem. 58, 575.
- Morrison, R.S. et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7537.
- Walicke, P. et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 3012.
- Grinspan, J.B. et al. (1993) J. Neurosci. Res. 36, 672.
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.
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.
- Ornitz, D.M. and Itoh, N. (2001) Genome Biol. 2, 3005.1.
- Fernig, D.G. and Gallagher, J.T. (1994) Prog. Growth Factor Res. 5, 353.
- Oda, Y. et al. (2004) J. Oral Maxillofac. Surg. 62, 73.
- Yetgin, S. et al. (2001) Leuk. Lymphoma 42, 83.
- Strutz, F. et al. (2002) Kidney Int. 61, 1714.
- Slavin, J. (1995) Cell Biol. Int. 19, 431.
- Bikfalvi, A. et al. (1997) Angiogenesis 1, 155.
- Bruno, E. et al. (1991) Blood 77, 2339.
- Huang, S. and Terstappen, L.W. (1992) Nature 360, 745.
- Bansal, R. and Pfeiffer, S.E. (1997) J. Neurosci. Res. 50, 215.
- Halaban, R. (1996) Semin. Oncol. 23, 673.
- Florkiewicz, R.Z. and Sommer. A. (1989) Proc. Nat. Acad. Sci. U.S.A. 86, 3978.
- Allouche, M. (1995) Leukemia 9, 937.
- Mignatti, P. et al. (1992) J. Cell Physiol. 151, 81.
- Jaye, M. et al. (1992) Biochim. Biophys. Acta. 1135, 185.
- Ornitz, D.M. (2000) BioEssays 22, 108.
- Bikfalvi, A. et al. (1997) Endocr. Rev. 18, 26.
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
Recombinant human FGF-b protein (#F-170) is a highly pure, recombinant, and biologically active protein.
Applications
Citations
Powered by Bioz- Skalecka, A. et al. (2016) Dev. Neurobiol. 76, 1308.
- Brazel, C.Y. et al. (2014) J. Neurochem. 128, 376.
- Birenboim, R. et al. (2013) J. Neurosci. Meth. 214, 9.
- Liu, X. et al. (2012) Neuropharmacology 62, 901.
- Zamburlin P. et al. (2012) Neurosci. Lett. 523, 30.
- Ziegler L. et al. (2011) Stem Cell Rev. and Rep. 7, 394.
- Ariano, P. et al. (2006) Cell Calcium 40, 63.
- Arriano, P. et al. (2005) J. Neurosci. Meth. 141, 271.
- Erriquez, J. et al. (2005) Neurosignals 14, 244.
- Vourc’h, P. et al. (2005) Biochem. Biophys. Res. Commun. 332, 215.
- Vourc’h, P. et al. (2004) Biochem. Biophys. Res. Commun. 317, 893.
- Lobner, D. and Ali, C. (2002) Brain Res. 954, 42.
- Romero-Ramos, M. et al. (2002) J. Neurosci. Res. 69, 894.
- Tejero-Diez, P. et al. (2000) Mol. Cell. Neurosci. 16, 766.
- Charon, I. et al. (1998) Neurochem. Int. 33, 503.
