Certificate of Analysis & Data Sheet

FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors. Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17250 Dalton. Human FGF2 is purified by proprietary chromatographic techniques.

E. coli

White lyophilized (freeze-dried) powder.

The protein was lyophilized from a concentrated (0.5 mg/ml) solution of PBS.

It is recommended to reconstitute the lyophilized hFGF-2 in water, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

Lyophilized hFGF-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution and filter sterilization hFGF-2 should be aliquoted and frozen. For long term storage and more diluted solutions it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

Greater than 98.0% as determined by:
(a) Gel filtration at non denaturing conditions using 25 nM Tris-HCl + 150 nM NaCl, pH 8.
(b) Analysis by reducing and non-reducing SDS-PAGE gel.

The sequence of the first six N-terminal amino acids was determined and was found to be MPALPE

Less than 10% dimers as determined by gel filtration chromatography and no agregates.

The was determined by the dose-dependant proliferation of mouse BALB/c 3T3 cells

Less than 0.05 ng/µg (0.5 EU/µg) of hFGF-2.

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.94 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

For research only