Recombinant Human FGF-12 Protein, CF


When Recombinant rhFGF R4/Fc Chimera (685-FR) is immobilized at 2 μg/mL (100 μL/well), it binds to Recombinant Human FGF-12 (Catalog # 2246-FG/CF) with an ED50 of 3-18 ng/mL.

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Recombinant Human FGF-12 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human FGFR4 Fc Chimera (Catalog # 685-FR) is immobilized at 2 μg/mL, 100 μL/well, Recombinant FGF-12 binds with an ED50 of 3-18 μg/mL.
E. coli-derived human FGF-12 protein
Accession #
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.


  • Bioactivity
Theoretical MW
20.4 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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2246-FG/CF in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA.
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.


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

Alternate Names for Recombinant Human FGF-12 Protein, CF

  • FGF12
  • FGF-12
  • FGF12B
  • FHF1
  • FHF-1
  • FHF1Fibroblast growth factor homologous factor 1
  • fibroblast growth factor 12
  • fibroblast growth factor 12B
  • fibroblast growth factor FGF-12b
  • Myocyte-activating factor


Fibroblast growth factor 12 (FGF-12) is a member of the FGF superfamily of molecules which contains at least 22 members. The FGFs are characterized by the presence of a core, 120 amino acid (aa) beta -trefoil structure, and all apparently bind heparin (1, 2). FGF-11, -12, -13, -14, originally termed FGF homologous factors (FHF) -3, -1, -2, -4, respectively, form a subgroup within the FGF family (1, 3). Human FGF-12/FHF-1 is synthesized as a 243 aa protein. It lacks a typical signal sequence and is considered to be a cytoplasmic protein. It does, however, possess an N-terminal bipartite nuclear localization signal (NLS) at aa 11-18 and 28-38 (4-6). The 243 aa protein has at least one alternate splice form that is 181 aa in length. This is termed FGF-12B. Alternate splicing deletes the N-terminal 66 aa in FGF-12 and replaces them with four aa in FGF-12B. This substitution removes the NLS from the short form. Studies on the short form (12B) show that it cannot bind any of the common FGF receptors. This is consistent with its cytoplasmic localization. It can, however, bind to IB2 (islet brain-2), a cellular kinase scaffold protein, and voltage-gated sodium channels, suggesting FGF-12B plays an important role in intracellular signaling and ion exchange (7). Mouse and human FGF-12B differ by only one amino acid.
  1. Itoh, N. and D.M. Ornitz (2004) Trends Genet. 20:563.
  2. Ornitz, D.M. and N. Itoh (2001) Genome Biol. 2:REVIEWS 3005.
  3. Green, P. et al. (1996) BioEssays 18:639.
  4. Smallwood, P. M. et al. (1996) Proc. Natl. Acad. Sci. 93:9850.
  5. Munoz-Sanjuan, I. et al. (2000) J. Biol. Chem 275:2589.
  6. Kok, L.D.S. et al. (1999) Biochem. Biophys. Res. Commun. 255:717.
  7. Olsen, S. K. et al. (2003) J. Biol. Chem. 278:34226.

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Gene Symbol FGF12