Recombinant Mouse FGF-9 Protein

Carrier Free

Catalog # Availability Size / Price Qty
7399-F9-025/CF

With Carrier

Catalog # Availability Size / Price Qty
7399-F9-025
R&D Systems Recombinant Proteins and Enzymes
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Citations (6)
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Recombinant Mouse FGF-9 Protein Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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 ED50 for this effect is 1.5‑7.5 ng/mL.
Source
E. coli-derived mouse FGF-9 protein
Met1-Ser208
Accession #
N-terminal Sequence
Analysis
Pro3
Structure / Form
Monomer
Predicted Molecular Mass
23.2 kDa
SDS-PAGE
24 kDa, reducing conditions

Product Datasheets

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7399-F9 (with carrier)

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7399-F9/CF (carrier free)

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.

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.
  • 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.

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.
  • 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.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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).

References
  1. Itoh, N. and D.M. Ornitz (2008) Dev. Dyn. 237:18.
  2. Miyamoto, M. et al. (1993) Mol. Cell. Biol. 13:4251.
  3. Santos-Ocampo, S. et al. (1996) J. Biol. Chem. 271:1726.
  4. Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
  5. Plotnikov, A.N. et al. (2001) J. Biol. Chem. 276:4322.
  6. Harada, M. et al. (2009) Nat. Genet. 41:289.
  7. Wu, X.L. et al. (2009) Am. J. Hum. Genet. 85:53.
  8. Colvin, J.S. et al. (1999) Dev. Dyn. 216:72.
  9. Lin, Y. et al. (2009) Dev. Biol. 329:44.
  10. Hung, I.H. et al. (2007) Dev. Biol. 307:300.
  11. Colvin, J.S. et al. (2001) Dev. Dyn 128:2095.
  12. Krejci, P. et al. (2009) Hum. Mutat. 30:1245.
  13. Leushacke, M. et al. (2011) PLoS ONE 6:e23381.
  14. Hendrix, N.D. et al. (2006) Cancer Res. 66:1354.
  15. Abdel-Rahman, W.M. et al. (2008) Hum. Mutat. 29:390.
Long Name
Fibroblast Growth Factor 9
Entrez Gene IDs
2254 (Human); 14180 (Mouse)
Alternate Names
FGF9; FGF-9; fibroblast growth factor 9 (glia-activating factor); Fibroblast growth factor 9; GAF; glia-activating factor; HBFG-9; HBGF-9; Heparin-binding growth factor 9; MGC119914; MGC119915; SYNS3

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.

6 Citations: Showing 1 - 6
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  1. 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
  2. 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
  3. 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
  4. 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
  5. 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
  6. 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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