Fibroblast Growth Factor, basic
human, recombinant, E. coli
For in vitro use only!
Shipping: shipped at ambient temperature
Storage Conditions: store at -20 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Weight: 17 kDa
Accession number: P09038
Accession number: P09038
Purity: > 95 % (SDS-PAGE, RP-HPLC)
Form: lyophilised (Recombinant FGF-2 was lyophilised from a 1 mg/ml solution in PBS pH 7.4)
Solubility: It is recommended to reconstitute the lyophilised FGF in sterile bidest H2O not less than 100 μg/ml, which can then be further diluted to other aqueous solutions. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Activity: ED50: < 0.5 ng/ml corresponding to a specific activity of 2 x 106 Units/mg, calculated by the dosedependent proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake).
FGF-2 is a single-chain polypeptide growth factor that plays a significant role in the process of wound healing and is a potent inducer of angiogenesis. Several different forms of the human protein exist ranging from 18-24 kDa in size due to the use of alternative start sites within the fgf-2 gene. It has a 55% amino acid residue identity to FGF-1 and has potent heparinbinding activity. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages. It was originally named basic fibroblast growth factor based upon its chemical properties and to distinguish it from acidic fibroblast growth factor. Other homologous FGFs belonging to the same family are int-2 (FGF-3), FGF-5, FGF-6, K-FGF, and KGF (keratinocyte growth factor, FGF-7). All factors are products of different genes, some of which are oncogene products (FGF-3, FGF-4, FGF-5). Recombinant Human FGF-basic (FGF-2) produced in E. coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17.35 kDa. Recombinant FGF-2 is purified by proprietary chromatographic techniques.
Sabbieti et al. (2005) Prostaglandins differently regulate FGF-2 and FGF receptor expression and induce nuclear translocation in osteoblasts via MAPK kinase. Cell Tissue Res. 319:267.
Frank et al. (2004) Effect of a dextran derivative associated with TGF-beta1 or FGF-2 on dermal fibroblast behaviour in dermal equivalents. J. Biomater. Sci. Polym. Ed. 15:1463.
Warzecha et al. (2004) Immunohistochemical expression of FGF-2, PDGF-A, VEGF and TGFbeta RII in the pancreas in the course of ischemia/reperfusion-induced acute pancreatitis. J. Physiol. Pharmacol. 55:791.
Hortala et al. (2004) Identification of c-Jun as a critical mediator for the intracrine 24 kDa FGF-2 isoform-induced cell proliferation. Int. J. Cancer 17; [Epub ahead of print].
Conconi et al. (2004) Ghrelin inhibits FGF-2-mediated angiogenesis in vitro and in vivo. Peptides 25:2179.
Chadi et al. (2004) FGF-2 and S100beta immunoreactivities increase in reactive astrocytes, but not in microglia, in ascending dopamine pathways following a striatal 6- OHDA-induced partial lesion of the nigrostriatal system. Cell Biol. Int. 28:849.