Recombinant Human FGF-3 Protein

Carrier Free

Catalog # Availability Size / Price Qty
1206-F3-025/CF

With Carrier

Catalog # Availability Size / Price Qty
1206-F3-025
R&D Systems Recombinant Proteins and Enzymes
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Citations (11)
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Recombinant Human FGF-3 Protein Summary

Product Specifications

Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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 0.02-0.1 µg/mL in the presence of 1 µg/mL of heparin.
Source
E. coli-derived human FGF-3 protein
Asp28-Arg212, with an N-terminal Met
Accession #
N-terminal Sequence
Analysis
Met
Predicted Molecular Mass
21.1 kDa

Product Datasheets

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1206-F3 (with carrier)

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1206-F3/CF (carrier free)

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.

1206-F3

Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, TCEP and EDTA with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile, deionized water.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

1206-F3/CF

Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, TCEP and EDTA.
Reconstitution Reconstitute at 100 μg/mL in sterile, deionized water.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
Reconstitution Calculator

Reconstitution Calculator

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Background: FGF-3

Fibroblast Growth Factor 3 (FGF-3) belongs to the large FGF family which has at least 23 members (1, 2). All FGF family members are heparin-binding growth factors with a core 120 amino acid (aa) FGF domain that allows for a common tertiary structure. FGFs are expressed during embryonic development and in restricted adult tissues. They act on cells of mesodermal and neuroectodermal origin to regulate diverse physiologic functions including angiogenesis, cell growth, pattern formation, embryonic development, metabolic regulation, cell migration, neurotrophic effects and tissue repair (3, 4). Signaling receptors for FGFs are type I transmembrane receptor tyrosine kinases belonging to the Ig superfamily. Four distinct but related classes of FGF receptors, FGF R1, 2, 3, and 4, exist. Through alternative splicing, multiple isoforms for FGF R1, 2 and 3, with distinct ligand recognition profiles, are also generated (4).

The FGF-3 gene, originally designated int-2, was first identified as a proto-oncogene activated in mouse mammary tumors by proviral integration (2). Amplification of this gene has also been found frequently in human tumors. Human FGF-3 cDNA predicts a 239 aa precursor protein with a 17 aa signal peptide and a 222 aa secreted mature protein with one potential N-linked glycosylation site (1). Human and mouse FGF-3 share 88% aa sequence identity. The Xenopus and mammalian secreted FGF-3 are processed proteolytically at both the N- and C-terminus (5). FGF-3 binds with high-affinity to the IIIb isoforms of FGF R1 and FGF R2. FGF-3 also binds the IIIc isoform of FGF R2, but with lower affinity (6). FGF-3 has been implicated in the induction of inner ear development (7). Studies have suggested that FGF-3 and FGF-8 function synergistically in otic placode induction and during neuronal development to regulate dorsoventral axis formation (8 - 10). During development, the activities of FGF-3 and FGF-8 are regulated negatively by the sprouty family proteins and by Sef (similar expression to fgf genes), a transmebrane protein that shares intracellular sequence similarities with the IL-17 receptor (10).

References
  1. Brookes, S. et al. (1989) Oncogene 4:429.
  2. Dickson, C. et al. (1989) Prog. Growth Factor Res. 1:123.
  3. Goldfarb, M. (1996) Cytokine and Growth Factor Reviews 7:311. 
  4. Green, P. et al. (1996) BioEssays 18:639.
  5. Antoine, M. et al. (2000) Cell Growth Differen. 11:593.
  6. Kohl, R. et al. (2002) J. Biol. Chem. 277:32760.
  7. Represa, J. et al. (1991) Nature 353:561.
  8. Maroon, H. et al. (2002) Development, 129:2099.
  9. Walshe, J. et al. (2002) Current Biol. 12:1117.
  10. Furthauer, M. et al. (2002) Nature Cell Biol. 4:170.
Long Name
Fibroblast Growth Factor 3
Entrez Gene IDs
2248 (Human)
Alternate Names
FGF3; FGF-3; fibroblast growth factor 3 (murine mammary tumor virus integration site (v-int-2) oncogene homolog); fibroblast growth factor 3; HBGF-3; Hst; INT-2; mouse; oncogene INT2

Citations for Recombinant Human FGF-3 Protein

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. Generation of Otic Lineages from Integration-Free Human-Induced Pluripotent Stem Cells Reprogrammed by mRNAs
    Authors: SL Boddy, R Romero-Gue, AR Ji, C Unger, L Corns, W Marcotti, MN Rivolta
    Stem Cells Int, 2020;2020(0):3692937.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Mutations of MAP1B encoding a microtubule-associated phosphoprotein cause sensorineural hearing loss
    Authors: L Cui, J Zheng, Q Zhao, JR Chen, H Liu, G Peng, Y Wu, C Chen, Q He, H Shi, S Yin, RA Friedman, Y Chen, MX Guan
    JCI Insight, 2020;5(23):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. 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
  4. Modeling human early otic sensory cell development with induced pluripotent stem cells
    Authors: H Lahlou, A Lopez-Juar, A Fontbonne, E Nivet, A Zine
    PLoS ONE, 2018;13(6):e0198954.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Barhl1 is required for the differentiation of inner ear hair cell-like cells from mouse embryonic stem cells
    Authors: C Zhong, Z Chen, X Luo, C Wang, H Jiang, J Shao, M Guan, L Huang, X Huang, J Wang
    Int. J. Biochem. Cell Biol., 2018;96(0):79-89.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Cell Culture
  6. HER2-overexpressing breast cancers amplify FGFR signaling upon acquisition of resistance to dual therapeutic blockade of HER2
    Authors: AB Hanker, JG Garrett, MV Estrada, PD Moore, PG Ericsson, JP Koch, E Langley, S Singh, PS Kim, GM Frampton, EM Sanford, P Owns, J Becker, MR Groseclose, S Castellino, H Joensuu, J Huober, JC Brase, M Samira, S Brohée, D Venet, D Brown, J Baselga, M Piccart, C Sotiriou, CL Arteaga
    Clin. Cancer Res., 2017;0(0):.
  7. Leading and trailing cells cooperate in collective migration of the zebrafish posterior lateral line primordium.
    Authors: Dalle Nogare D, Somers K, Rao S, Matsuda M, Reichman-Fried M, Raz E, Chitnis A
    Development, 2014;141(16):3188-96.
    Species: Zebrafish
    Sample Types: Whole Organism
    Applications: In Vivo
  8. Human marrow stromal cells downsize the stem cell fraction of lung cancers by fibroblast growth factor 10.
    Authors: Kanehira M, Kikuchi T, Santoso A, Tode N, Hirano T, Ohkouchi S, Tamada T, Sugiura H, Harigae H, Ichinose M
    Mol Cell Biol, 2014;34(15):2848-56.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. A gradient of Bmp7 specifies the tonotopic axis in the developing inner ear.
    Authors: Mann Z, Thiede B, Chang W, Shin J, May-Simera H, Lovett M, Corwin J, Kelley M
    Nat Commun, 2014;5(0):3839.
    Species: Chicken
    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. Platelet-derived growth factor receptor regulates salivary gland morphogenesis via fibroblast growth factor expression.
    Authors: Yamamoto S, Fukumoto E, Yoshizaki K, Iwamoto T, Yamada A, Tanaka K, Suzuki H, Aizawa S, Arakaki M, Yuasa K, Oka K, Chai Y, Nonaka K, Fukumoto S
    J. Biol. Chem., 2008;283(34):23139-49.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: Bioassay

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