Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 0.2‑1.0 ng/mL.
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
18.8 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.
SDS-PAGE
19 kDa, reducing conditions
Publications
Read Publication using 5750-F6/CF in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, Ammonium Sulfate, EDTA, DTT.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse FGF-6 Protein, CF
FGF6
FGF-6
fibroblast growth factor 6
HBGF-6
Heparin secretory-transforming protein 2
Heparin-binding growth factor 6
HST2
HST-2
HSTF2
HSTF-2
Background
Fibroblast Growth Factor-6 (FGF-6), also known as HST-2, is a 25 - 28 kDa member of the FGF family of heparin binding polypeptides which are potent regulators of cell proliferation, differentiation, and function. FGF proteins contain a 120 amino acid (aa) core FGF domain that exhibits a beta -trefoil structure (1, 2). Mature mouse FGF-6 is a 171 aa protein that shares 94% and 99% aa sequence identity with human and rat FGF-6, respectively (3). It binds and signals primarily through FGF R1c, 2c, and 4 (4). FGF-6 functions as a mitogen for fibroblasts, vascular endothelial cells, and prostate carcinoma cells, and N-linked glycosylation is required for the full mitogenic effect (5 - 7). FGF-6 expression is restricted to skeletal muscle during development, although it can be upregulated in prostate cancer and Kaposi sarcoma (7 - 9). In the adult, FGF-6 is upregulated in injured skeletal muscle and is required for muscle regeneration (10). FGF-6 inhibits the terminal differentiation of myoblasts and also cooperates with TGF-beta 2 to promote chondrogenesis in embryonic somites (8, 11).
Wiedlocha, A. and V. Sorensen (2004) Curr. Top. Microbiol. Immunol. 286:45.
Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
de Lapeyriere, O. et al. (1990) Oncogene 5:823.
Ornitz, D.M. et al. (1996) J. Biol. Chem. 271:15292.
Pizette, S. et al. (1991) Cell Growth Differ. 2:561.
Asada, M. et al. (1999) Growth Factors 16:293.
Ropiquet, F. et al. (2000) Cancer Res. 60:4245.
de Lapeyriere, O. et al. (1993) Development 118:601.
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