Recombinant Human/Mouse FGF-8b Protein, CF

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Recombinant Human/Mouse FGF-8b (Catalog # 423-F8/CF) stimulates cell proliferation in the NR6R‑3T3 mouse fibroblast cell line. The ED50 for this effect is 6.5-40 ng/mL in the presence of 1 μg/mL heparin.
1 μg/lane of Recombinant Human/Mouse FGF-8b was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 23 kDa.

Product Details

Summary
Reactivity Hu, MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Catalog# & Formulation Size Price

Recombinant Human/Mouse FGF-8b Protein, CF 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 typically 6.5-40 ng/mL in the presence of 1 µg/mL heparin.
Source
E. coli-derived FGF-8 protein
Gln23-Arg215, with an N-terminal Met
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Proteins
Gene
FGF8
Purity
>97%, 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

Theoretical MW
22.5 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
23 kDa, reducing condtions
Publications
Read Publications using
423-F8/CF 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.
  • 3 months, 2 to 8 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and Brij-35.
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human/Mouse FGF-8b Protein, CF

  • 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

Background

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 (1-3). Alternate splicing of mouse FGF-8 mRNA generates eight secreted isoforms, designated a-h, but 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 (30 aa for FGF-8b; 20 aa for the shortest, FGF-8a), 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). Mouse FGF-8b shares 100% aa identity with human FGF-8b. 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. FGF-8b shows the strongest receptor affinity and oncogenic transforming capacity although FGF-8a and FGF-8e are also transforming and have been found in human prostate, breast or ovarian tumors (1, 5, 9-12). 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, 9, 13).

  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 Tiss. Res. 313:139.
  3. Tanaka, A. et al. (1992) Proc. Natl. Acad. Sci. USA 89:8928.
  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. Ghosh, A.K. et al. (1996) Cell Growth Differ. 7:1425.
  10. Mattila, M.M. et al. (2001) Oncogene 20:2791.
  11. Valve, E. et al. (2000) Int. J. Cancer 88:718.
  12. Valve, E.M. et al. (2001) Lab. Invest. 81:815.
  13. Nezu, M. et al. (2005) Biochem. Biophys. Res. Commun. 335:843.

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423-F8/CF
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Applications: Bioactivity

Publications for FGF-8 (423-F8/CF)(37)

We have publications tested in 8 confirmed species: Human, Mouse, Rat, Avian - Quail, Chicken, Rabbit, Xenopus, Zebrafish.

We have publications tested in 4 applications: Bioassay, Expansion/Differentiation, In Ovo, In Vivo.


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Bioassay
(27)
Expansion/Differentiation
(1)
In Ovo
(1)
In Vivo
(8)
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Human
(10)
Mouse
(9)
Rat
(3)
Avian - Quail
(1)
Chicken
(8)
Rabbit
(1)
Xenopus
(2)
Zebrafish
(3)
All Species
Showing Publications 1 - 10 of 37. Show All 37 Publications.
Publications using 423-F8/CF Applications Species
X Hu, JW Lee, X Zheng, J Zhang, X Lin, Y Song, B Wang, X Hu, HH Chang, Y Chen, CP Lin, Y Zhang Efficient induction of functional ameloblasts from human keratinocyte stem cells Stem Cell Res Ther, 2018;9(1):126. 2018 [PMID: 29720250] (Bioassay, Human) Bioassay Human
G Shall, M Menosky, S Decker, P Nethala, R Welchko, X Leveque, M Lu, M Sandstrom, U Hochgeschw, J Rossignol, G Dunbar Effects of Passage Number and Differentiation Protocol on the Generation of Dopaminergic Neurons from Rat Bone Marrow-Derived Mesenchymal Stem Cells Int J Mol Sci, 2018;19(3):. 2018 [PMID: 29498713] (Bioassay, Rat) Bioassay Rat
T Johansen, C Krabbe, SI Schmidt, AM Serrano, M Meyer Comparative Analysis of Spontaneous and Stimulus-Evoked Calcium Transients in Proliferating and Differentiating Human Midbrain-Derived Stem Cells Stem Cells Int, 2017;2017(0):9605432. 2017 [PMID: 29201062] (Bioassay, Human) Bioassay Human
AR Rodrigues, N Yakushiji-, Y Atsuta, G Andrey, P Schorderet, D Duboule, CJ Tabin Integration of Shh and Fgf signaling in controlling Hox gene expression in cultured limb cells Proc. Natl. Acad. Sci. U.S.A, 2017;0(0):. 2017 [PMID: 28270602] (Bioassay, Chicken) Bioassay Chicken
SA Liddelow, KA Guttenplan, LE Clarke, FC Bennett, CJ Bohlen, L Schirmer, ML Bennett, AE Mnch, WS Chung, TC Peterson, DK Wilton, A Frouin, BA Napier, N Panicker, M Kumar, MS Buckwalter, DH Rowitch, VL Dawson, TM Dawson, B Stevens, BA Barres Neurotoxic reactive astrocytes are induced by activated microglia Nature, 2017;541(7638):481-487. 2017 [PMID: 28099414] (Bioassay, Human) Bioassay Human
Florian Wegner Neuronal Dysfunction in iPSC-Derived Medium Spiny Neurons from Chorea-Acanthocytosis Patients Is Reversed by Src Kinase Inhibition and F-Actin Stabilization J. Neurosci., 2016;36(47):12027-12043. 2016 [PMID: 27881786] (Bioassay, Human) Bioassay Human
Fibulin-1 Binds to Fibroblast Growth Factor 8 with High Affinity: Effects on Embryo Survival J Biol Chem, 2016;0(0):. 2016 [PMID: 27402846] (Bioassay, Human) Bioassay Human
Daniel A Monti N-Acetyl Cysteine May Support Dopamine Neurons in Parkinson&#039;s Disease: Preliminary Clinical and Cell Line Data PLoS ONE, 2016;11(6):e0157602. 2016 [PMID: 27309537] (Bioassay, Human) Bioassay Human
Eva Hedlund Dopamine Receptor Antagonists Enhance Proliferation and Neurogenesis of Midbrain Lmx1a-expressing Progenitors Sci Rep, 2016;6(0):26448. 2016 [PMID: 27246266] (Bioassay, Mouse) Bioassay Mouse
Chan W, Howe K, Clegg J, Guimond S, Price D, Turnbull J, Pratt T 2-O Heparan Sulfate Sulfation by Hs2st Is Required for Erk/Mapk Signalling Activation at the Mid-Gestational Mouse Telencephalic Midline. PLoS ONE, 2015;10(6):e0130147. 2015 [PMID: 26075383] (Bioassay, Mouse) Bioassay Mouse
Show All 37 Publications.

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Bioinformatics

Gene Symbol FGF8
Entrez
Uniprot