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Recombinant Human FGF-9 Protein, Fc Tag, 100 µg  

Recombinant Human FGF-9 Protein, Fc Tag, 100 µg

Recombinant human FGF9 Fc chimera, Leu4-Ser208, produced in human HEK293 cells, Fc Tag

Synonym: Recombinant human protein,FGF9,GAF,HBFG-9

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Availability: within 7 days

264,00 €

Fibroblast growth factor 9 is also known as FGF9, GAF, HBFG-9, SYNS3, and is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 is also a mitogen for oligodendrocyte type 2 astrocyte progenitor cells, smooth muscle cells, pheochromocytoma PC12 cells, and BALB/3T3 fibroblasts. However, unlike FGF acidic and basic, FGF9 has no effect on human umbilical vein endothelial cells, and it has been demonstrated that FGF9 binds preferentially to the IIIc form of FGFR3. Although no typical signal sequence was found in FGF9, it is secreted efficiently after synthesis not in a conventional manner. In nervous system, FGF9 is produced mainly by neurons and may plays an important role in CNS development. FGF9 has been shown to interact with Fibroblast growth factor receptor 3.

Recombinant human FGF9 Fc chimera (rhFGF9-Fc) Leu4-Ser208 (Accession # AAI03979) was produced in human HEK293 cells

Molecular Characterization
Human FGF-9, Fc Tag is fused with a human IgG1 Fc tag at the N-terminus, and has a calculated MW of 50.6 kDa. The predicted N-terminus is Glu. As a result of glycosylation, DTT-reduced Protein migrates as 55 kDa and non-reduced protein migrates as 110 kDa in SDS-PAGE .

Less than 1.0 EU per μg of the Human FGF-9, Fc Tag by the LAL method.

>92% as determined by SDS-PAGE.

Lyophilized from 0.22 μm filtered solution in 50 mM tris, 100 mM glycine, pH7.5. Normally Mannitol or Trehalose are added as protectants before lyophilization.

See Certificate of Analysis for reconstitution instructions and specific concentrations.

Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C).


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(2) Santos-Ocampo S, et al. 1996, J Biol Chem., 271(3):1726-31.
(3) Chellaiah A, et al. 1999, J. Biol. Chem. (UNITED STATES) 274 (49): 34785–94.