Recombinant Human FGF-3 Protein
R&D Systems, part of Bio-Techne | Catalog # 1206-F3
Key Product Details
Product Specifications
Source
Asp28-Arg212, with an N-terminal Met
Purity
Endotoxin Level
N-terminal Sequence Analysis
Predicted Molecular Mass
Activity
The ED50 for this effect is 0.02-0.1 µg/mL in the presence of 1 µg/mL of heparin.
Formulation, Preparation and Storage
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.
Carrier: 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.
|
Carrier Free: 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.
|
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
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Brookes, S. et al. (1989) Oncogene 4:429.
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Dickson, C. et al. (1989) Prog. Growth Factor Res. 1:123.
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Goldfarb, M. (1996) Cytokine and Growth Factor Reviews 7:311.
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Green, P. et al. (1996) BioEssays 18:639.
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Antoine, M. et al. (2000) Cell Growth Differen. 11:593.
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Kohl, R. et al. (2002) J. Biol. Chem. 277:32760.
- Represa, J. et al. (1991) Nature 353:561.
- Maroon, H. et al. (2002) Development, 129:2099.
- Walshe, J. et al. (2002) Current Biol. 12:1117.
- Furthauer, M. et al. (2002) Nature Cell Biol. 4:170.
Long Name
Alternate Names
Entrez Gene IDs
Gene Symbol
UniProt
Additional FGF-3 Products
Product Documents for Recombinant Human FGF-3 Protein
Product Specific Notices for Recombinant Human FGF-3 Protein
For research use only