Bovine FGF-2 (basic)
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| Cat-Nr. | B30-004 |
| Size | 50 µg |
| Price | 185 € |
| Source | E. coli |
| Formulation | lyophilized |
| Purity Confirmation | > 98% by SDS-PAGE |
| Length [aa] | 145 |
| Molecular Weight | 16.34 kDa |
| Endotoxin Levels | < 0.1 ng per µg of bovine FGF-2 |
| Biological Activity | The ED50 for stimulation of cell proliferation in human umbilical vein endothelial cells (HUVEC) by bovine FGF-2 has been determined to be in the range of 0.1-2 ng/ml. |
| Species Reactivity | Bovine |
| Buffer | 0.5X PBS |
| Reconstitution | The bovine FGF-2 is supplied in lyophilized form and can be reconstituted with ddH2O at 50 µg/mL. This solution can be diluted into other buffered solutions or stored frozen for future use. For long term storage we would recommend to add at least 0.1% human or bovine serum albumin. |
| Stability and Storage | The lyophilized bovine FGF-2, though stable at room temperature, is best stored in working aliquots at -20°C to -70°C |
| Synonyms | Fgf2; bFGF; Fgf-2 |
| Description | FGF2 (basic) is one of at least 23 mitogenic proteins of the FGF family, which show 35-60% amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. Storage pools within the cell or on cell surface heparan sulfate proteoglycans (HSPG) are likely. FGF2 has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum and placenta. This factor contains four cysteine residues but reduced FGF2 retains full biological activity, indicating that disulfide bonds are not required for this activity. Several reports indicate that a variety of forms of FGF2 are produced as a result of N-terminal extensions. These extensions apparently affect localization of FGF2 in cellular compartments but do not affect biological activity. Studies indicate that binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and show a similar range of biological activities. FGF2 stimulates the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin. The cells include fibroblasts, endothelial cells, astrocytes, oligodendrocytes, neuroblasts, keratinocytes, osteoblasts, smooth muscle cells, and melanocytes. FGF2 is chemotactic and mitogenic for endothelial cells in vitro. FGF2 induces neuron differentiation, survival and regeneration. The 17 kDa bovine sequence has 95% aa identity with human and sheep FGF basic. |
| Protein Sequence | AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYS SWYVALKRTG QYKLGPKTGP GQKAILFLPM SAKS |
| Uniprot ID | P03969 |
| Protein RefSeq | NP_776481.2 |
| mRNA RefSeq | NM_174056 |
Figures
SDS-PAGE analysis of recombinant bovine FGF-2 (basic). Samples were loaded in 15% SDS-polyacrylamide gel under reducing and non-reducing condition and stained with Coomassie blue.
FGF2-induced proliferation of primary normal human dermal fibroblasts. NHDF cells were stimulated with increasing amounts of bovine FGF-2 (basic).
FGF2-induced proliferation of primary human umbilical vein endothelial cells. HUVECs were stimulated with increasing amounts of bovine FGF-2 (basic).
Proliferation assay with NHDF. The cells were stimulated with increasing amounts of recombinant human, mouse, rat and bovine FGF-2. Values are the means (±SD) of triplicate determinations and expressed as percentage of control.
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