Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein Best Seller
R&D Systems, part of Bio-Techne | Catalog # 232-FA
Key Product Details
Product Specifications
Source
Phe16-Asp155, with an N-terminal Met
Purity
Endotoxin Level
N-terminal Sequence Analysis
Predicted Molecular Mass
Activity
The ED50 for this effect is 0.015-0.15 ng/mL in the presence of 10 µg/mL of heparin.
Reviewed Applications
Read 1 review rated 4 using 232-FA in the following applications:
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: 232-FA
Formulation | Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
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.
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Carrier Free: 232-FA/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
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.
|
Background: FGF acidic/FGF1
FGF acidic, also known as FGF1, ECGF, and HBGF-1, is a 17 kDa nonglycosylated member of the FGF family of mitogenic peptides. FGF acidic, which is produced by multiple cell types, stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It plays a number of roles in development, regeneration, and angiogenesis (1-3). Human FGF acidic shares 54% amino acid sequence identity with FGF basic and 17%‑33% with other human FGFs. It shares 92%, 96%, 96%, and 96% aa sequence identity with bovine, mouse, porcine, and rat FGF acidic, respectively, and exhibits considerable species crossreactivity. Alternate splicing generates a truncated isoform of human FGF acidic that consists of the N-terminal 40% of the molecule and functions as a receptor antagonist (4). During its nonclassical secretion, FGF acidic associates with S100A13, copper ions, and the C2A domain of synaptotagmin 1 (5). It is released extracellularly as a disulfide-linked homodimer and is stored in complex with extracellular heparan sulfate (6). The ability of heparan sulfate to bind FGF acidic is determined by its pattern of sulfation, and alterations in this pattern during embryogenesis thereby regulate FGF acidic bioactivity (7). The association of FGF acidic with heparan sulfate is a prerequisite for its subsequent interaction with FGF receptors (8, 9). Ligation triggers receptor dimerization, transphosphorylation, and internalization of receptor/FGF complexes (10). Internalized FGF acidic can translocate to the cytosol with the assistance of Hsp90 and then migrate to the nucleus by means of its two nuclear localization signals (11-13). The phosphorylation of FGF acidic by nuclear PKC delta triggers its active export to the cytosol where it is dephosphorylated and degraded (14, 15). Intracellular FGF acidic functions as a survival factor by inhibiting p53 activity and proapoptotic signaling (16).
References
- Jaye, M. et al. (1986) Science 233:541.
- Galzie, Z. et al. (1997) Biochem. Cell Biol. 75:669.
- Presta, M. et al. (2005) Cytokine Growth Factor Rev. 16:159.
- Yu, Y.L. et al. (1992) J. Exp. Med. 175:1073.
- Rajalingam, D. et al. (2007) Biochemistry 46:9225.
- Guerrini, M. et al. (2007) Curr. Pharm. Des. 13:2045.
- Allen, B.L. and A.C. Rapraeger (2003) J. Cell Biol. 163:637.
- Robinson, C.J. et al. (2005) J. Biol. Chem. 280:42274.
- Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
- Wiedlocha, A. and V. Sorensen (2004) Curr. Top. Microbiol. Immunol. 286:45.
- Wesche, J. et al. (2006) J. Biol. Chem. 281:11405.
- Imamura, T. et al. (1990) Science 249:1567.
- Wesche, J. et al. (2005) Biochemistry 44:6071.
- Wiedlocha, A. et al. (2005) Mol. Biol. Cell 16:794.
- Nilsen, T. et al. (2007) J. Biol. Chem. 282:26245.
- Bouleau, S. et al. (2005) Oncogene 24:7839.
Long Name
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Gene Symbol
UniProt
Additional FGF acidic/FGF1 Products
Product Documents for Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein
Product Specific Notices for Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein
For research use only