Recombinant Human FGF-8a Protein, CF

Catalog # Availability Size / Price Qty
Recombinant Human FGF-8a Protein Bioactivity
2 Images
Product Details
Citations (11)
Supplemental Products

Recombinant Human FGF-8a Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
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 0.25-1.5 μg/mL in the presence of 10 µg/mL heparin.
E. coli-derived human FGF-8 protein
Gln23-Arg204, with an N-terminal Met
Accession #
N-terminal Sequence
Predicted Molecular Mass
21 kDa

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, and EDTA.
Reconstitution Reconstitute at 500 μg/mL in sterile PBS.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.

Data Images

Bioactivity Recombinant Human FGF-8a Protein Bioactivity View Larger

Recombinant Human FGF-8a (Catalog # 4745-F8) stimulates cell proliferation of the NR6R‑3T3 mouse fibroblast cell line. The ED50 for this effect is 0.25-1.5 μg/mL in the presence of 10 μg/mL heparin.

SDS-PAGE Recombinant Human FGF-8a Protein SDS-PAGE View Larger

1 μg/lane of Recombinant Human FGF-8a was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 22 kDa.

Reconstitution Calculator

Reconstitution Calculator

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Background: FGF-8

FGF-8 is a member of the fibroblast growth factor family that was originally discovered as a growth factor essential for the androgen-dependent growth of mouse mammary carcinoma cells (1-4). Alternate splicing of mouse FGF-8 mRNA generates eight secreted isoforms, designated a-h. Only FGF-8a, b, e and f exist in humans (4). FGF-8 contains a 22 amino acid (aa) signal sequence, an N-terminal domain that varies according to the isoform (20 aa for FGF-8a, which is the shortest), a 125 aa FGF domain and a 37 aa proline-rich C-terminal sequence. The FGF domain of FGF-8 shares the most aa identity with FGF17 (75%) and FGF-18 (67%), and the three form an FGF subfamily (2). Human FGF-8a shares 100% aa identity with mouse, rat and bovine FGF-8a, and 99%, 83%, 83% and 78% aa identity with canine, Xenopus, chicken and zebrafish FGF-8a, respectively. FGF-8 is widely expressed during embryogenesis, and mediates epithelial-mesenchymal transitions. It plays an organizing and inducing role during gastrulation, and regulates patterning of the midbrain/hindbrain, eye, ear, limbs and heart in the embryo (2, 5-8). The isoforms may play different roles in development. For example, FGF-8a expands the midbrain in transgenic mice, while FGF-8b transforms midbrain into cerebellum (5). FGF-8 activates the ‘c’ splice forms of fibroblast growth factor receptors FGF R2, FGF R3, and FGF R4, with differential activity among the FGF-8 isoforms (2, 9). FGF-8b shows the strongest receptor affinity and oncogenic transforming capacity, although FGF-8a and e are also transforming and have been found in human prostate, breast or ovarian tumors (1, 5, 10 - 13). FGF-8 shows limited expression in the normal adult, but low levels are found in the reproductive and genitourinary tract, peripheral leukocytes and bone marrow hematopoietic cells (3, 10, 14).

  1. Mattila, M.M. and P.L. Harkonen (2007) Cytokine Growth Factor Rev. 18:257.
  2. Reuss, B. and O. von Bohlen und Halbach (2003) Cell Tissue Res. 313:139.
  3. Payson, R.A. et al. (1996) Oncogene 13:47.
  4. Gemel, J. et al. (1996) Genomics 35:253.
  5. Olsen, S.K. et al. (2006) Genes Dev. 20:185.
  6. Crossley, P.H. et al. (1996) Cell, 84:127.
  7. Heikinheimo, M. et al. (1994) Mech. Dev. 48:129.
  8. Sun, X. et al. (1999) Genes Dev. 13:1834.
  9. Blunt, A.G. et al. (1997) J. Biol. Chem. 272:3733.
  10. Ghosh, A.K. et al. (1996) Cell Growth Differ. 7:1425.
  11. Mattila, M.M. et al. (2001) Oncogene 20:2791.
  12. Valve, E. et al. (2000) Int. J. Cancer 88:718.
  13. Valve, E.M. et al. (2001) Lab. Invest. 81:815.
  14. Nezu, M. et al. (2005) Biochem. Biophys. Res. Commun. 335:843.
Long Name
Fibroblast Growth Factor 8
Entrez Gene IDs
2253 (Human); 14179 (Mouse); 29349 (Rat)
Alternate Names
AIGF; AIGFKAL6; Androgen-induced growth factor; FGF8; FGF-8; fibroblast growth factor 8 (androgen-induced); fibroblast growth factor 8; HBGF-8; Heparin-binding growth factor 8; MGC149376

Citations for Recombinant Human FGF-8a Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

11 Citations: Showing 1 - 10
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  1. Defective metabolic programming impairs early neuronal morphogenesis in neural cultures and an organoid model of Leigh syndrome
    Authors: G Inak, A Rybak-Wolf, P Lisowski, TM Pentimalli, R Jüttner, P Glažar, K Uppal, E Bottani, D Brunetti, C Secker, A Zink, D Meierhofer, MT Henke, M Dey, U Ciptasari, B Mlody, T Hahn, M Berruezo-L, N Karaiskos, M Di Virgili, JA Mayr, SB Wortmann, J Priller, M Gotthardt, DP Jones, E Mayatepek, W Stenzel, S Diecke, R Kühn, EE Wanker, N Rajewsky, M Schuelke, A Prigione
    Nature Communications, 2021;12(1):1929.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Identification of ASCL1 as a determinant for human iPSC-derived dopaminergic neurons
    Authors: AM Earley, LF Burbulla, D Krainc, R Awatramani
    Scientific Reports, 2021;11(1):22257.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Single-Cell Transcriptomics of Parkinson's Disease Human In�Vitro Models Reveals Dopamine Neuron-Specific Stress Responses
    Authors: HJR Fernandes, N Patikas, S Foskolou, SF Field, JE Park, ML Byrne, AR Bassett, E Metzakopia
    Cell Rep, 2020;33(2):108263.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. A monolayer hiPSC culture system for autophagy/mitophagy studies in human dopaminergic neurons
    Authors: P Stathakos, N Jiménez-Mo, LA Crompton, PA Nistor, JL Badger, PA Barbuti, TL Kerrigan, AD Randall, MA Caldwell, JD Lane
    Autophagy, 2020;0(0):1-17.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Defects in mRNA Translation in LRRK2-Mutant hiPSC-Derived Dopaminergic Neurons Lead to Dysregulated Calcium Homeostasis
    Authors: JW Kim, X Yin, A Jhaldiyal, MR Khan, I Martin, Z Xie, T Perez-Rose, M Kumar, L Abalde-Atr, J Xu, L Chen, SM Eacker, DJ Surmeier, NT Ingolia, TM Dawson, VL Dawson
    Cell Stem Cell, 2020;27(4):633-645.e7.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Felodipine induces autophagy in mouse brains with pharmacokinetics amenable to repurposing
    Authors: FH Siddiqi, FM Menzies, A Lopez, E Stamatakou, C Karabiyik, R Ureshino, T Ricketts, M Jimenez-Sa, MA Esteban, L Lai, MD Tortorella, Z Luo, H Liu, E Metzakopia, HJR Fernandes, A Bassett, E Karran, BL Miller, A Fleming, DC Rubinsztei
    Nat Commun, 2019;10(1):1817.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Fibroblast growth factor 8b induces uncoupling protein 1 expression in epididymal white preadipocytes
    Authors: S Westphal, T Gantert, C Kless, K Hüttinger, M Klingenspo, T Fromme
    Sci Rep, 2019;9(1):8470.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Human iPSC-Derived Neural Progenitors Are an Effective Drug Discovery Model for Neurological mtDNA Disorders
    Authors: C Lorenz, P Lesimple, R Bukowiecki, A Zink, G Inak, B Mlody, M Singh, M Semtner, N Mah, K Aur‚, M Leong, O Zabiegalov, EM Lyras, V Pfiffer, B Fauler, J Eichhorst, B Wiesner, N Huebner, J Priller, T Mielke, D Meierhofer, Z Izsv k, JC Meier, F Bouillaud, J Adjaye, M Schuelke, EE Wanker, A LombŠs, A Prigione
    Cell Stem Cell, 2017;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Physiological characterisation of human iPS-derived dopaminergic neurons.
    Authors: Hartfield, Elizabet, Yamasaki-Mann, Michiko, Ribeiro Fernandes, Hugo J, Vowles, Jane, James, William, Cowley, Sally A, Wade-Martins, Richard
    PLoS ONE, 2014;9(2):e87388.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  10. Altered splicing of FGFR1 is associated with high tumor grade and stage and leads to increased sensitivity to FGF1 in bladder cancer.
    Authors: Tomlinson DC, Knowles MA
    Am. J. Pathol., 2010;177(5):2379-86.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Similar expression to FGF (Sef) inhibits fibroblast growth factor-induced tumourigenic behaviour in prostate cancer cells and is downregulated in aggressive clinical disease.
    Authors: Darby S, Murphy T, Thomas H, Robson CN, Leung HY, Mathers ME, Gnanapragasam VJ
    Br. J. Cancer, 2009;101(11):1891-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay


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