Species : |
Human |
Source : |
E.coli |
Tag : |
Non |
Description : |
FGF basic is a member of the FGF family of at least 23 related mitogenic proteins which show 35 - 60% amino acid conservation. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF basic 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 FGF basic retains full biological activity, indicating that disulfide bonds are not required for this activity. A variety of forms of FGF basic are produced as a result of N-terminal extensions. These extensions affect l centigradealization of FGF basic in cellular compartments but do not affect biological activity. 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. FGF basic stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. FGF basic induces neuron differentiation, survival, and regeneration. FGF basic also modulates embryonic development and differentiation. These observed in vitro functions of FGF basic suggest FGF basic may play a role in vivo in the modulation of such normal pr centigradeesses as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, and neuronal function and neural degeneration. Additionally, FGF basic may participate in the production of a variety of pathological conditions resulting from excessive cell proliferation and excessive angiogenesis. |
Form : |
Supplied as a 0.2 μm filtered solution (145 μL) in 10 mM Sodium Phosphate and 0.3 M glycerin (pH 7.0) containing 50 μg of bovine serum albumin per 1 μg of the cytokine at a concentration of 0.172 mg/mL. |
Bio-activity : |
The biological activity of recombinant human FGF basic was monitored in a mitogenic assay by measuring the FGF basic dependent 3H-thymidine incorporation in quiescent NR6R-3T3 fibroblasts (Rizzino, A. et al., 1988. Cancer Research 48:4266 - 4271). The ED50 for this effect is typically 0.1 - 0.25 ng/mL. |
Molecular Mass : |
The 157 amino acid residue recombinant protein has a molecular mass of 17.4 kDa. |
Endotoxin : |
< 1.0 eu per 1 μg of the cytokine as determined by the lal |
Purity : |
>97%, as determined by SDS-PAGE and visualized by silver stain. |
Usage : |
FOR RESEARCH USE ONLY |
Quality Control Test : |
Samples are stable for greater than six months at -20 centigrade to -70 centigrade in a manual defrost freezer. Upon thawing, this cytokine can be stored under sterile conditions at 2 - 8 centigrade for one month or at -20 centigrade to -70 centigrade in a manual defrost freezer for three months without detectable loss of activity. |
Concentration : |
0.172 mg/mL |
Warning : |
Avoid repeated freeze-thaw cycles. |