Recombinant Human FGF-9 Protein Summary
Additional Information |
Sf21-Expressed |
Details of Functionality |
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. Rubin, J.S. et al. (1991) Proc. Natl. Acad. Sci. USA 88:415. The ED 50 for this effect is 1-5 ng/mL. |
Source |
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human FGF-9 protein Met1-Ser208 & Ala2-Ser208 |
Accession # |
|
N-terminal Sequence |
Met1 & Ala2 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
FGF9 |
Purity |
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<1.0 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
23 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 |
Multiple bands between 22-29 kDa, reducing conditions |
Publications |
Read Publications using 273-F9 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. 3 months, 2 to 8 degreesC under sterile conditions after reconstitution. |
Buffer |
Lyophilized from a 0.2 μm filtered solution in MOPS, Na 2 SO 4 and EDTA with BSA as a carrier protein. |
Purity |
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human FGF-9 Protein
Background
FGF-9 (fibroblast growth factor-9), also called HBGF-9 (heparin-binding growth factor-9) and GAF (glia-activating factor), is an approximately 26 kDa secreted glycoprotein of the FGF family (1-3). FGFs exhibit heparin-dependent regulation of cell proliferation, differentiation, and function, and are characterized by a core heparin-binding FGF domain of approximately 120 amino acids (aa) that exhibits a beta -trefoil structure (1). FGF-9, -16 and -20 form a subfamily that shares 65-71% aa sequence identity, binds FGF R3 (IIIb), and are efficiently secreted despite having an uncleavable, bipartite signal sequence (1-3). Secreted human FGF-9 is a 205-207 aa protein that lacks the N-terminal 1-3 aa and shares 98% sequence identity with mouse, rat, equine, porcine and bovine FGF-9. In addition to FGF R3 (IIIb), FGF-9 binding to the IIIc splice forms of FGF R1, R2 and R3 are variably reported (3-5). An unusual constitutive dimerization of FGF-9 buries receptor interaction sites which lowers its activity, and increases heparin affinity which inhibits diffusion (4-6). A spontaneous mouse mutant, Eks, interferes with dimerization, resulting monomeric, diffusible FGF-9 that causes elbow and knee synostoses (joint fusions) due to FGF-9 misexpression in developing joints (6). In humans, FGF-9 mutations that lower receptor binding cause multiple synostoses syndrome (SYNS) (7). Expression in brain and kidney are reported in the adult rat (2, 8). In the mouse embryo the location and timing of FGF-9 expression affects development of the skeleton, cerebellum, lungs, heart, vasculature, digestive tract, and testes (1, 6-11). Deletion of mouse FGF-9 is lethal at birth due to lung hypoplasia, and causes rhizomelia, or shortening of the proximal skeleton (1, 10, 11). Altered FGF-9 expression or function is reported in human colon, endometrial, and ovarian cancers, correlating with progression, invasiveness, and survival (12-15).
- Itoh, N. and D.M. Ornitz (2008) Dev. Dyn. 237:18.
- Miyamoto, M. et al. (1993) Mol. Cell. Biol. 13:4251.
- Santos-Ocampo, S. et al. (1996) J. Biol. Chem. 271:1726.
- Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
- Plotnikov, A.N. et al. (2001) J. Biol. Chem. 276:4322.
- Harada, M. et al. (2009) Nat. Genet. 41:289.
- Wu, X.L. et al. (2009) Am. J. Hum. Genet. 85:53.
- Colvin, J.S. et al. (1999) Dev. Dyn. 216:72.
- Lin, Y. et al. (2009) Dev. Biol. 329:44.
- Hung, I.H. et al. (2007) Dev. Biol. 307:300.
- Colvin, J.S. et al. (2001) Dev. Dyn 128:2095.
- Krejci, P. et al. (2009) Hum. Mutat. 30:1245.
- Leushacke, M. et al. (2011) PLoS ONE 6:e23381.
- Hendrix, N.D. et al. (2006) Cancer Res. 66:1354.
- Abdel-Rahman, W.M. et al. (2008) Hum. Mutat. 29:390.
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