hFGFbasic
- 貨號 Cat. No.
- F-170
- 規格 Size
- 5 μg 5x5 μg
Description
hFGFbasic
Human Fibroblast Growth Factor-basic
| Product#: | F-170 |
| Sizes: |
| 5 mg |
| 5 x 5 mg |
| Preparation: |
| hFGF-b is a recombinant growth factor produced in E. coli. |
| M.W.: |
| 17 kDa (155 amino acids). |
| Purity: |
| Greater than 95% pure as estimated by SDS-PAGE and HPLC analysis. |
| Bioassay: |
The activity of this lot was determined by its ability to increase thymidine incorporation in BaF3 cells (ED>0.5ng/ml). And by its ability to induce proliferation of 3T3-L1 cells, measured by XTT assay. |
 | hFGF Basic (# F-170 ) promote proliferation of 3T3-L1 cells. 3T3-L1 were cultured with 10% bovine serum for 24 h then the serum reduced to 0.5% and the cells were stimulated with increased concentrations of Basic hFGF. The cell proliferation was measured 2 days post stimulation using XTT method. |
| Locus Link ID: | 2247. |
| References: |
1. | Ornitz, D.M. and Itoh, N. (2001) Genome Biology 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. | Florkiewicz, R.Z. and Sommer. A. (1989) Proc. Nat. Acad. Sci. USA 86, 3978. |
9. | Allouche, M. (1995) Leukemia 9, 937. |
10. | Mignatti, P. et al. (1992) J. Cell Physiol. 151, 81. |
11. | Jaye, M. et al. (1992) Biochim. Biophys. Acta. 1135, 185. |
12. | Ornitz, D.M (2000) BioEssays 22, 108. |
13. | Bikfalvi, A. et al. (1997) Endocr. Rev. 18, 26. |
14. | Bruno, E. et al. (1991) Blood 77, 2339. |
15. | Huang, S. and Terstappen, L.M.M. (1992) Nature 360, 745. |
16. | Bansal, R. and Pfeiffer, S.E. (1997) J. Neurosci. Res. 50, 215. |
17. | Halaban, R. (1996) Semin. Oncol. 23, 673. |
Fibroblast growth factor-basic (FGF-b, FGF-2) belongs to the 22 member FGF family.1 FGFs play major roles in development,2 wound healing,3 hematopoiesis,4 tumorigenesis,5 and angiogenisis.6 It is expressed mostly in tissues of mesoderm and neuroectoderm origin.7
FGF-b 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-b 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 consist 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-b to its receptor is regulated by heparan sulfate proteoglycans.12
FGF-b is implicated in many biological processes. It has been shown to induce endothelial cell proliferation, migration and angiogensis in vitro and in vivo,13 to stimulate myeloid progenitors,14 to stimulate stromal growth,15 to promote the release of endothelium from its connective tissue anchor (thus encouraging the entry of new vascular endothelium),6 to regulate oligodendrocyte progenitor proliferation and differentiation in culture,16 and to play a role in the autonomous growth of melanoma cells.17
FGF-b 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-b 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 consist 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-b to its receptor is regulated by heparan sulfate proteoglycans.12
FGF-b is implicated in many biological processes. It has been shown to induce endothelial cell proliferation, migration and angiogensis in vitro and in vivo,13 to stimulate myeloid progenitors,14 to stimulate stromal growth,15 to promote the release of endothelium from its connective tissue anchor (thus encouraging the entry of new vascular endothelium),6 to regulate oligodendrocyte progenitor proliferation and differentiation in culture,16 and to play a role in the autonomous growth of melanoma cells.17