Recombinant Human FGF-9 Protein

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Recombinant human FGF-9 (273-F9) induces proliferation in the Balb/3T3 mouse embryonic fibroblast cell line. The ED50 for this effect is 1-5 ng/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Catalog# & Formulation Size Price

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 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

Dilutions
  • Bioactivity
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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Publications for FGF-9 (273-F9)(41)

We have publications tested in 7 confirmed species: Human, Mouse, Rat, Bovine, Chicken, Feline, Transgenic Human.

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


Filter By Application
Bioassay
(36)
Cell Culture
(4)
In Vivo
(1)
All Applications
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Human
(26)
Mouse
(9)
Rat
(2)
Bovine
(1)
Chicken
(1)
Feline
(1)
Transgenic Human
(1)
All Species
Showing Publications 1 - 10 of 41. Show All 41 Publications.
Publications using 273-F9 Applications Species
J Jansen, KC Reimer, JS Nagai, FS Varghese, GJ Overheul, M de Beer, R Roverts, D Daviran, LAS Fermin, B Willemsen, M Beukenboom, S Djudjaj, S von Stillf, LE van Eijk, M Mastik, M Bulthuis, WD Dunnen, H van Goor, JL Hillebrand, SH Triana, T Alexandrov, MC Timm, BT van den Be, M van den Br, Q Nlandu, J Heijnert, EMJ Bindels, RM Hoogenboez, F Mooren, C Kuppe, P Miesen, K Grünberg, T Ijzermans, EJ Steenberge, J Czogalla, MF Schreuder, N Sommerdijk, A Akiva, P Boor, VG Puelles, J Floege, TB Huber, COVID Moon, RP van Rij, IG Costa, RK Schneider, B Smeets, R Kramann SARS-CoV-2 infects the human kidney and drives fibrosis in kidney organoids Cell Stem Cell, 2021;29(2):217-231.e8. 2021 [PMID: 35032430] (Bioassay, Human) Bioassay Human
R Ungricht, L Guibbal, MC Lasbennes, V Orsini, M Beibel, A Waldt, R Cuttat, W Carbone, A Basler, G Roma, F Nigsch, JS Tchorz, D Hoepfner, PS Hoppe Genome-wide screening in human kidney organoids identifies developmental and disease-related aspects of nephrogenesis Cell Stem Cell, 2021;0(0):. 2021 [PMID: 34847364] (Bioassay, Human) Bioassay Human
JOR Hernandez, X Wang, M Vazquez-Se, M Lopez-Marf, MF Sobral-Rey, A Moran-Horo, M Sundberg, DO Lopez-Cant, CK Probst, GU Ruiz-Espar, K Giannikou, R Abdi, EP Henske, DJ Kwiatkowsk, M Sahin, DR Lemos A tissue-bioengineering strategy for modeling rare human kidney diseases in vivo Nature Communications, 2021;12(1):6496. 2021 [PMID: 34764250] (Bioassay, Human) Bioassay Human
K Sasaki, A Oguchi, K Cheng, Y Murakawa, I Okamoto, H Ohta, Y Yabuta, C Iwatani, H Tsuchiya, T Yamamoto, Y Seita, M Saitou The embryonic ontogeny of the gonadal somatic cells in mice and monkeys Cell Reports, 2021;35(5):109075. 2021 [PMID: 33951437] (Bioassay, Human) Bioassay Human
Y Yamamura, K Furuichi, Y Murakawa, S Hirabayash, M Yoshihara, K Sako, S Kitajima, T Toyama, Y Iwata, N Sakai, K Hosomichi, PM Murphy, A Tajima, K Okita, K Osafune, S Kaneko, T Wada Identification of candidate PAX2-regulated genes implicated in human kidney development Scientific Reports, 2021;11(1):9123. 2021 [PMID: 33907292] (Bioassay, Human) Bioassay Human
M Chiara Per, N Bellitto, ERS Maylem, F Caloni, LJ Spicer Effects of selected hormones and their combination on progesterone and estradiol production and proliferation of feline granulosa cells cultured in�vitro Theriogenology, 2021;168(0):1-12. 2021 [PMID: 33826978] (Bioassay, Feline) Bioassay Feline
SE Howden, SB Wilson, E Groenewege, L Starks, TA Forbes, KS Tan, JM Vanslambro, EM Holloway, YH Chen, S Jain, JR Spence, MH Little Plasticity of distal nephron epithelia from human kidney organoids enables the induction of ureteric tip and stalk Cell Stem Cell, 2020;0(0):. 2020 [PMID: 33378647] (Bioassay, Transgenic Human) Bioassay Transgenic Human
K Uchimura, H Wu, Y Yoshimura, BD Humphreys Human Pluripotent Stem Cell-Derived Kidney Organoids with Improved Collecting Duct Maturation and Injury Modeling Cell Reports, 2020;33(11):108514. 2020 [PMID: 33326782] (Bioassay, Human) Bioassay Human
IM Knarston, S Pachernegg, G Robevska, I Ghobrial, PX Er, E Georges, M Takasato, AN Combes, A Jørgensen, MH Little, AH Sinclair, KL Ayers An In�Vitro Differentiation Protocol for Human Embryonic Bipotential Gonad and Testis Cell Development Stem Cell Reports, 2020;15(6):1377-1391. 2020 [PMID: 33217324] (Cell Culture, Human) Cell Culture Human
S Ettou, YL Jung, T Miyoshi, D Jain, K Hiratsuka, V Schumacher, ME Taglienti, R Morizane, PJ Park, JA Kreidberg Epigenetic transcriptional reprogramming by WT1 mediates a repair response during podocyte injury Sci Adv, 2020;6(30):eabb5460. 2020 [PMID: 32754639] (Bioassay, Human) Bioassay Human
Show All 41 Publications.

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Bioinformatics

Gene Symbol FGF9
Uniprot