Recombinant Human FGF-5 Protein, CF


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Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human FGF-5 Protein, CF Summary

Details of Functionality
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Rizzino, A. et al. (1988) Cancer Res. 48:4266; Thomas, K. et al. (1987) Methods Enzymol. 147:120. The ED50 for this effect is 2-10 ng/mL in the presence of 1 µg/mL of heparin.
E. coli-derived human FGF-5 protein
Glu23-Gly268 (Lys238Asn and Pro245Ser), with an N-terminal Met & Leu26-Gly268 (Lys238Asn and Pro245Ser)
Accession #
N-terminal Sequence
Met & Leu26
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


Theoretical MW
27 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
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237-F5/CF in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
Supplied as a 0.2 μm filtered solution in MOPS, Na2SO4, EDTA and DTT.
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human FGF-5 Protein, CF

  • FGF5
  • FGF-5
  • fibroblast growth factor 5
  • HBGF-5
  • Heparin-binding growth factor 5
  • Smag-82


The FGF family is comprised of at least seven polypeptides that are potent regulators of cell proliferation, differentiation and function. All FGFs have two conserved cysteine residues and share 30 - 50% sequence homology at the amino acid level. FGF-5 was originally identified as a transforming gene by the NIH-3T3 focus formation assay using DNA derived from human tumors. FGF-5 cDNA encodes a 267 amino acid residue protein with a putative 22 amino acid residue signal peptide. The murine homologue of FGF-5 was cloned and found to be 84% homologous to the human protein at the amino acid sequence level. Human and murine FGF-5 exhibit cross species activity.

In vitro, rhFGF-5 is a mitogen for Balb/3T3 fibroblasts and bovine heart endothelial cells. FGF-5 was also reported to be a major muscle-derived survival factor for cultured spinal motoneurons. In vivo, FGF-5 is suggested to play important roles in both embryology and neurobiology. Developmentally, FGF-5 mRNA is initially found in the embryoblast followed by the lateral somatic mesoderm, where it may play a role in angiogenesis, plus the myotomes cranial to the tail region, where it may delay terminal myoblast differentiation during cell migration. FGF-5 continues to impact muscle post-natally where it is believed to function as a target-derived neurotrophic factor of skeletal muscle. In the nervous system, FGF-5 has been most often identified in neurons associated with the limbic system, notably in neurons of the olfactory bulb and pyramidal cells of the hippocampus. Hippocampal FGF-5 is suggested to serve as a neurotrophic and differentiative factor for cholinergic and serotonergic neurons projecting to this region.

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Publications for FGF-5 (237-F5/CF)(4)

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Gene Symbol FGF5