Recombinant Mouse FGF-9 Protein Summary
Product Specifications
Met1-Ser208
Analysis
Product Datasheets
Carrier Free
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.
7399-F9
Formulation | Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA with BSA as a carrier protein. |
Reconstitution | Reconstitute at 250 μg/mL in sterile, deionized water. |
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.
|
7399-F9/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA. |
Reconstitution | Reconstitute at 250 μg/mL in sterile, deionized water. |
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.
|
Reconstitution Calculator
Background: FGF-9
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 mouse FGF-9 is a 205‑207 aa protein that lacks the N-terminal 1-3 aa and shares >98% sequence identity with rat, human, 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.
Citations for Recombinant Mouse FGF-9 Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 6
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Mapping Somatosensory Afferent Circuitry to Bone Identifies Neurotrophic Signals Required for Fracture Healing
Authors: Xu, M;Thottappillil, N;Cherief, M;Li, Z;Zhu, M;Xing, X;Gomez-Salazar, M;Mwirigi, JM;Sankaranarayanan, I;Tavares-Ferreira, D;Zhang, C;Wang, XW;Archer, M;Guan, Y;Tower, RJ;Cahan, P;Price, TJ;Clemens, TL;James, AW;
bioRxiv : the preprint server for biology
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Low retinoic acid levels mediate regionalization of the Sertoli valve in the terminal segment of mouse seminiferous tubules
Authors: K Imura-Kish, A Uchida, N Tsunekawa, H Suzuki, HM Takase, Y Hirate, M Kanai-Azum, R Hiramatsu, M Kurohmaru, Y Kanai
Scientific Reports, 2021-01-13;11(1):1110.
Species: Mouse
Sample Types: In Vivo
Applications: Bioassay -
Hierarchical patterning modes orchestrate hair follicle morphogenesis
Authors: JD Glover, KL Wells, F Matthäus, KJ Painter, W Ho, J Riddell, JA Johansson, MJ Ford, CAB Jahoda, V Klika, RL Mort, DJ Headon
PLoS Biol., 2017-07-11;15(7):e2002117.
Species: Mouse
Sample Types: Whole Tissue
Applications: Bioassay -
Application of VEGFA and FGF-9 enhances angiogenesis, osteogenesis and bone remodeling in type 2 diabetic long bone regeneration.
Authors: Wallner C, Schira J, Wagner J, Schulte M, Fischer S, Hirsch T, Richter W, Abraham S, Kneser U, Lehnhardt M, Behr B
PLoS ONE, 2015-03-05;10(3):e0118823.
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo -
Fibroblast growth factor 9 activates akt and MAPK pathways to stimulate steroidogenesis in mouse leydig cells.
Authors: Lai, Meng-Sha, Cheng, Yu-Sheng, Chen, Pei-Rong, Tsai, Shaw-Jen, Huang, Bu-Miin
PLoS ONE, 2014-03-06;9(3):e90243.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Factors expressed by murine embryonic pancreatic mesenchyme enhance generation of insulin-producing cells from hESCs.
Authors: Guo T, Landsman L, Li N, Hebrok M
Diabetes, 2013-01-10;62(5):1581-92.
Species: Mouse
Sample Types: Whole Tissue
Applications: Bioassay
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