Recombinant Human FGF basic/FGF2/bFGF, 145 aa TC Grade, CF Summary
Additional Information |
Analyzed by SEC-MALS |
Details of Functionality |
The protein is used at 20 ng/mL to support a 100-fold expansion of rat cortical neural stem cells or mouse cortical stem cells over 3 passages. Cells were cultured in N2 plus medium and supplemented with FGF basic every day. Measured in a cell proliferation assay using NR6R-3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED 50 for this effect is 0.3-3 ng/mL. |
Source |
E. coli-derived human FGF basic/FGF2/bFGF protein Ala144-Ser288 |
Accession # |
|
N-terminal Sequence |
Ala144 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
FGF2 |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
16 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. |
Publications |
Read Publications using 4114-TC in the following applications:
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Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution. |
Buffer |
Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl. |
Reconstitution Instructions |
Reconstitute at 0.5-1.0 mg/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 FGF basic/FGF2/bFGF, 145 aa TC Grade, CF
Background
FGF basic (also known as FGF2 and HBGF-2) is an 18-34 kDa, heparin-binding member of the FGF superfamily of molecules (1-3). Superfamily members are characterized by the presence of a centrally placed beta -trefoil structure. FGF acidic (FGF1) and FGF basic (FGF2) were the first two identified FGFs, and the designations acidic and basic refer to their relative isoelectric points. Human FGF basic is 288 amino acids (aa) in length. There are multiple start sites, four of which utilize atypical CUG codons, and one that initiates at an AUG start site (4-6). The four CUG start sites generate high molecular weight (HMW) FGF basic. There is a 34 kDa, 288 aa form, a 24 kDa, 210 aa form, a 22.5 kDa, 201 aa form, and a 22 kDa, 196 aa form. All are retained intracellularly, undergo extensive methylation, and possess one or more nuclear localization signals (NLS) (7-9). The AUG initiating form is 18 kDa and 155 aa in length. There is no signal sequence (ss). It is, however, secreted directly through the plasma membrane via a mechanism that appears to be dependent upon tertiary structure (10). In place of a ss, there is purportedly a 9 aa N-terminal prosegment that precedes a 146 aa mature segment (11). Early isolations of 18 kDa bovine FGF basic yielded 146 aa molecules, an effect attributed to the presence of acid proteases (12). The molecule contains a heparin-binding site (aa residues 128-144), and undergoes phosphorylation at Ser117 (13). There is also an ill-defined C-terminal NLS that may be more “functional” (or 3-dimensional) than structural (7). Human 146 aa FGF basic is 97% aa identical to mouse FGF basic (14).
- Sorenson, V. et al. (2006) BioEssays 28:504.
- Kardami, E. et al. (2004) Cardiovasc. Res. 63:458.
- Nugent, M.A. and R.V. Lozzo (2000) Int. J. Biochem. Cell Biol. 32:115.
- Abraham, J.A. et al. (1986) EMBO J. 5:2523.
- Prats, H. et al. (1989) Proc. Natl. Acad. Sci. USA 86:1836.
- Arnaud, E. et al. (1999) Mol. Cell. Biol. 19:505.
- Foletti, A. et al. (2003) Cell. Mol. Life Sci. 60:2254.
- Arese, M. et al. (1999) Mol. Biol. Cell 10:1429.
- Pintucci, G. et al. (1996) Mol. Biol. Cell 7:1249.
- Nickel, W. (2005) Traffic 6:607.
- SwissProt # P09038.
- Klagsbrun, M. et al. (1987) Proc. Natl. Acad. Sci. USA 84:1839.
- Bailly, K. et al. (2000) FASEB J. 14:333.
- Hebert, J.M. et al. (1990) Dev. Biol. 138:454.
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