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Recombinant Human FGF-4 (aa 71-206) Protein

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human FGF-4 (aa 71-206) Protein Summary

Details of Functionality
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 0.25-1.25 ng/mL.
Source
E. coli-derived human FGF-4 protein
Ser71-Leu206 with an N-terminal Met
Accession #
N-terminal Sequence
Met is predicted: No results obtained, sequencing might be blocked
Structure / Form
Monomer
Protein/Peptide Type
Recombinant Proteins
Gene
FGF4
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
15.2 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.
SDS-PAGE
14 kDa, reducing conditions
Publications
Read Publications using
7460-F4 in the following applications:

Packaging, Storage & Formulations

Storage
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.

Notes

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

Alternate Names for Recombinant Human FGF-4 (aa 71-206) Protein

  • FGF4
  • FGF-4
  • fibroblast growth factor 4
  • HBGF-4
  • HBGF-4Transforming protein KS3
  • heparin secretory transforming protein 1
  • Heparin secretory-transforming protein 1
  • Heparin-binding growth factor 4
  • HST-1
  • HST-1HSTF-1
  • HSTF1fibroblast growth factor 4 splice isoform
  • HSTFGF-4
  • human stomach cancer, transforming factor from FGF-related oncogene
  • kaposi sarcoma oncogene
  • KFGF
  • K-FGF
  • KS3
  • oncogene HST

Background

FGF‑4 (fibroblast growth factor‑4), also known as FGF-K or K‑FGF (Kaposi’s sarcoma-associated FGF), is a 25 kDa secreted, heparin‑binding member of the FGF family (1, 2). The human FGF‑4 cDNA encodes 206 amino acids (aa) with a 33 aa signal sequence and a 173 aa mature protein with an FGF homology domain that contains a heparin binding region near the C‑terminus (2). Mature human FGF‑4 (aa 71‑206) shares 91%, 82%, 94% and 91% aa identity with mouse, rat, canine and bovine FGF‑4, respectively. Human FGF‑4 has been shown to exhibit cross species activity. Expression of FGF-4 and its receptors, FGF R1c, 2c, 3c and 4, is spatially and temporally regulated during embryonic development (1, 3). Its expression in the mouse trophoblast inner cell mass promotes expression of FGF R2, and is required for maintenance of the trophectoderm and primitive endoderm (3‑5). Later in mouse development, FGF‑4 works together with FGF‑8 to mediate the activities of the apical ectodermal ridge, which direct the outgrowth and patterning of vertebrate limbs (3, 6‑9). FGF-4 is proposed to play a physiologically relevant role in human embryonic stem cell self-renewal. It promotes stem cell proliferation, but may also aid differentiation depending on context and concentration, and is often included in embryonic stem cell media in vitro (10‑12). A C‑terminally truncated 15 kDa isoform that opposes full‑length FGF‑4 and promotes differentiation is endogenously expressed in human embryonic stem cells. FGF‑4 is mitogenic for fibroblasts and endothelial cells in vitro and has autocrine transforming potential (13). It is a potent angiogenesis promoter in vivo and has been investigated as therapy for coronary artery disease (14).

  1. Reuss, B. and O. von Bohlen und Halbach (2003) Cell Tiss. Res. 313:139.
  2. Hebert, J.M. et al. (1990) Dev. Biol. 138:454.
  3. Niswander, L. and G.R. Martin (1992) Development 114:755.
  4. Feldman, B. et al. (1995) Science 267:246.
  5. Goldin, S.N. and V.E. Papaioannou (2003) Genesis 36:40.
  6. Sun, X. et al. (2002) Nature 418:501.
  7. Boulet, A.M. et al. (2004) Dev. Biol. 273:361.
  8. Yu, K and D.M. Ornitz (2008) Development 135:483.
  9. Mariani, F.V. et al. (2008) Nature 453:401.
  10. Johannesson, M. et al. (2009) PLoS ONE 4:e4794.
  11. Kunath, T. et al. (2007) Development 134:2895.
  12. Mayshar, Y. et al. (2008) Stem Cells 26:767.
  13. Hajitou, A. et al. (1998) Oncogene 17:2059.
  14. Flynn, A. and T. O’Brien (2008) IDrugs 11:283.

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Publications for FGF-4 (7460-F4)(2)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 2 applications: Bioassay, Differentiation.


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Bioassay
(1)
Differentiation
(2)
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(2)
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Bioinformatics

Gene Symbol FGF4
Uniprot