Recombinant Human FGF-basic/FGF2

Recombinant(E.coli)

Lyophilizate,sterile-filtered

Cat.No.     RP1002-10UG                 10μg               store at -20℃

Cat.No.     RP1002-50UG                 50μg               store at -20℃

Synonyms :  Fibroblast Growth Factor-basic, FGF-2, HBGF-2, HBGH-2, FGF-b, Prostatropin

Description:  Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.4KDalton.The FGF2 is purified by proprietary chromatographic techniques.

Source:        Escherichia Coli.

Purity:         Greater than 90.0% as determined by SDS-PAGE.

Endotoxin Level : Endotoxin level is less than 0.1 ng per μg (1EU/μg) as determined  by the LAL method.

Biological Activity : The ED50, measured in a mitogenic assay using quiescent NR6R-3T3 fibroblasts was found to be less then 0.1 ng/ml, corresponding to a specific activity of 3 x 10⁶ Units/mg.

Amino acid sequence: GSMAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS

Formulation: The FGF2 was lyophilized from sterile PBS , pH 7.4.

Solubility: It is recommended to reconstitute the lyophilized FGF2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability: Lyophilized FGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -20°C. Upon reconstitution FGF2 should be stored at 4°C between 2-7 days and for future use below -20°C.
          For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles. Recommend to aliquot the protein into smaller quantities for optimal storage.

Usage: Follow the instructions on the vial. Centrifuge the vial at 4℃ before opening to recover the entire contents.

The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Background

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 localization 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 processes 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.

References: 

1. Coulier, F. et al., 1997, J. Mol. Evol. 44:43.

2. Chen, C.H. et al., 2004, Curr. Vasc. Pharmacol. 2:33.

3. Mohammadi, M. et al., 2005, Curr. Opin. Struct. Biol. 15:506.

4. Fernig, D. et al., 1994, Prog. Growth Factor Res. 5:353.