Recombinant Human FGF-9 Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human FGF-9 Protein Summary

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 ED50 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

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:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, 2 to 8 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 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

  • 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

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).

  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.

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273-F9
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Publications for FGF-9 (273-F9)(30)

We have publications tested in 5 confirmed species: Human, Mouse, Rat, Bovine, Chicken.

We have publications tested in 3 applications: Bioassay, Cell Culture, In Vivo.


Filter By Application
Bioassay
(26)
Cell Culture
(3)
In Vivo
(1)
All Applications
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Human
(17)
Mouse
(9)
Rat
(2)
Bovine
(1)
Chicken
(1)
All Species
Showing Publications 1 - 10 of 30. Show All 30 Publications.
Publications using 273-F9 Applications Species
Kumar Gupta A, Sarkar P, Wertheim J, Pan X, Carroll T, Oxburgh L Asynchronous mixing of kidney progenitor cells potentiates nephrogenesis in organoids. Commun Biol, 0;3(1):231. 0 [PMID: 32393756] (Bioassay, Human) Bioassay Human
M Grosch, S Ittermann, E Rusha, T Greisle, C Ori, DJ Truong, AC O'Neill, A Pertek, GG Westmeyer, M Drukker Nucleus size and DNA accessibility are linked to the regulation of paraspeckle formation in cellular differentiation BMC Biol., 2020;18(1):42. 2020 [PMID: 32321486] (Cell Culture, Human) Cell Culture Human
M Asakawa, M Itoh, T Suganami, T Sakai, S Kanai, I Shirakawa, X Yuan, T Hatayama, S Shimada, Y Akiyama, K Fujiu, Y Inagaki, I Manabe, S Yamaoka, T Yamada, S Tanaka, Y Ogawa Upregulation of cancer-associated gene expression in activated fibroblasts in a mouse model of non-alcoholic steatohepatitis Sci Rep, 2019;9(1):19601. 2019 [PMID: 31862949] (Bioassay, Human) Bioassay Human
S Bijland, G Thomson, M Euston, K Michail, K Thümmler, S Mücklisch, CL Crawford, SC Barnett, M McLaughlin, TJ Anderson, C Linington, ER Brown, ER Kalkman, JM Edgar An in vitro model for studying CNS white matter: functional properties and experimental approaches F1000Res, 2019;8(0):117. 2019 [PMID: 31069065] (Bioassay, Mouse) Bioassay Mouse
H Murata, T Tsuzuki, T Kido, M Kakita-Kob, N Kida, Y Hisamatsu, H Okada Progestin-induced heart and neural crest derivatives-expressed transcript 2 inhibits angiopoietin 2 via fibroblast growth factor 9 in human endometrial stromal cells Reprod Biol, 2019;0(0):. 2019 [PMID: 30852242] (Bioassay, Human) Bioassay Human
WKW Ho, L Freem, D Zhao, KJ Painter, TE Woolley, EA Gaffney, MJ McGrew, A Tzika, MC Milinkovit, P Schneider, A Drusko, F Matthäus, JD Glover, KL Wells, JA Johansson, MG Davey, HM Sang, M Clinton, DJ Headon Feather arrays are patterned by interacting signalling and cell density waves PLoS Biol., 2019;17(2):e3000132. 2019 [PMID: 30789897] (Bioassay, Chicken) Bioassay Chicken
H Wu, K Uchimura, EL Donnelly, Y Kirita, SA Morris, BD Humphreys Comparative Analysis and Refinement of Human PSC-Derived Kidney Organoid Differentiation with Single-Cell Transcriptomics Cell Stem Cell, 2018;0(0):. 2018 [PMID: 30449713] (Bioassay, Human) Bioassay Human
CW van den Be, L Ritsma, MC Avramut, LE Wiersma, BM van den Be, DG Leuning, E Lievers, M Koning, JM Vanslambro, AJ Koster, SE Howden, M Takasato, MH Little, TJ Rabelink Renal Subcapsular Transplantation of PSC-Derived Kidney Organoids Induces Neo-vasculogenesis and Significant Glomerular and Tubular Maturation In�Vivo Stem Cell Reports, 2018;0(0):. 2018 [PMID: 29503086] (Bioassay, Human) Bioassay Human
LF Schütz, RE Hurst, NB Schreiber, LJ Spicer Transcriptome profiling of bovine ovarian theca cells treated with fibroblast growth factor 9 Domest. Anim. Endocrinol., 2018;63(0):48-58. 2018 [PMID: 29413902] (Cell Culture, Human) Cell Culture Human
KE Tumelty, N Higginson-, X Fan, P Bajaj, KM Knowlton, M Shamashkin, AJ Coyle, W Lu, SP Berasi Identification of direct negative crosstalk between the SLIT2 and Bone Morphogenetic Protein-Gremlin signaling pathways J. Biol. Chem., 2018;0(0):. 2018 [PMID: 29317497] (Bioassay, Human) Bioassay Human
Show All 30 Publications.

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Bioinformatics

Gene Symbol FGF9
Uniprot