Recombinant Equine FGF Basic Protein

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DataSheet   

The recombinant equine FGFb protein is derived from in vivo expression of equine FGFb gene in E. coli and purified using his-tag affinity column and can be used in multiple applications such as cell culture, ELISA and western blot.

Alternative names for FGF basic: basic fibroblast growth factor, FGF2, FGF-b

This product is for Laboratory Research Use Only not for diagnostic and therapeutic purposes or any other purposes.

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Description

Genorise Recombinant Equine FGF Basic Protein Summary

Alternative names for FGF basic: basic fibroblast growth factor, FGF2, FGF-b

 

Product Specifications

Purity > 95%, by SDSPAGE under reducing conditions and visualized by silver stain.
Endotoxin Level < 0.1 EU per 1 μg of the protein by the LAL method.
Activity Measured in a cell proliferation assay using NR6R-3T3 mouse fibroblast cells. Raines EW et al. (1985) Methods Enzymol. 109:749.

The ED50 for this effect is typically 0.1-0.6 ng/mL

Background: 

Basic fibroblast growth factor, also known as bFGF, FGF2 or FGF-β, is a member of the fibroblast growth factor family (1). In normal tissue, basic fibroblast growth factor is present in basement membranes and in the subendothelial extracellular matrix of blood vessels. It stays membrane-bound as long as there is no signal peptide. It has been hypothesized that, during both wound healing of normal tissues and tumor development, the action of heparan sulfate-degrading enzymes activates bFGF, thus mediating the formation of new blood vessels, a process known as angiogenesis. bFGF has been shown in preliminary animal studies to protect the heart from injury associated with a heart attack, reducing tissue death and promoting improved function after reperfusion (2). Recent evidence has shown that low levels of FGF2 play a key role in the incidence of excessive anxiety. Basic fibroblast growth factor has been shown to interact with casein kinase 2, alpha 1(3), RPL6 (4) and ribosomal protein S19 (5).

References

  1. Kim HS (1998). Cytogenet. Cell Genet. 83 (1-2): 73.
  2. House SL, et al. (2003). Circulation 108 (1): 3140.
  3. Skjerpen, et al. EMBO J. (England) 21 (15): 4058.
  4. Shen, B, et al. Biochem. Biophys. Res. Commun. (UNITED STATES) 252 (2): 524.
  5. Soulet, F, et al. Biochem. Biophys. Res. Commun. (United States) 289 (2): 591.

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