ProDots Recombinant Human FGF-3 Protein Summary
Pre-aliquoted, lyophilized protein dots for use in cell culture mediumFeatures and Benefits
- Rolls out of bottle for easy cell culture medium preparation
- Eliminates time spent aliquoting
- One protein dot can be used to make 500 mL of 10 ng/mL cell culture medium
Asp28 - Arg212, with an N-terminal Met
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.
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.
|Reconstitution||For a stock solution, reconstitute at 100 μg/mL in sterile PBS, or simply roll ProDot® directly to the medium for immediate use.
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
• 6 months from date of receipt at room temperature.
• 12 months from date of receipt at 2-8 °C as supplied.
• 1 month at 2-8 °C under sterile conditions after reconstitution.
• 3 months at -20 to -80 °C under sterile conditions after reconstitution.
ProDots®Recombinant Human FGF-3 stimulated cell proliferation of the NR6R-3T3 mouse fibroblast cell line. The ED50for this effect is 0.02-0.1 μg/mL.
1 μg/lane of ProDots®Recombinant Human FGF-3 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized with silver staining, showing a single band at 21 kDa.
Fibroblast growth factor 3 (FGF-3) belongs to the large FGF family which has at least 23 members. 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. 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.
The FGF-3 gene, originally designated int-2, was first identified as a proto-oncogene activated in mouse mammary tumors by proviral integration. 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. 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. 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. FGF-3 has been implicated in the induction of inner ear development. Recent studies have suggested that FGF-3 and FGF-8 function synergistically in otic placode induction and during neuronal development to regulate dorsoventral axis formation. 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 transmembrane protein that shares intracellular sequence similarities with the IL-17 receptor.
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