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Recombinant Mouse FGFR3 alpha (IIIb) Fc Chimera Protein, CF

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Recombinant Mouse FGF R3 (IIIb) Fc Chimera (Catalog # 9089-FR) inhibits Recombinant Mouse FGF acidic (Catalog # 4686-FA)-dependent proliferation of Human FGF R3 (IIIc) transfected BaF3 mouse pro‑B cells. The ED50 for ...read more

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse FGFR3 alpha (IIIb) Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit FGF acidic-dependent proliferation of BaF3 mouse pro‑B cells transfected with human FGF R3 (IIIc). The ED50 for this effect is 0.2-1.2 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse FGF R3 protein
Mouse FGF R3 (IIIb)
(Ala33-Tyr369)
Accession # NP_001156689
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Ala33
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Fgfr3
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
63 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
83-101 kDa, reducing conditions

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.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse FGFR3 alpha (IIIb) Fc Chimera Protein, CF

  • CD333
  • CEK
  • EC 2.7.10
  • FGF R3
  • FGFR3
  • fibroblast growth factor receptor 3
  • HSFGFR3EX
  • JTK4
  • JTK4thanatophoric dwarfism

Background

Fibroblast growth factor receptor 3 (FGF R3), also known as CEK2 and CD333, is an approximately 120 kDa transmembrane receptor tyrosine kinase that plays a role in skeletal development and tumorigenesis (1). Mature mouse FGF R3 (IIIc) consists of a 349 amino acid (aa) extracellular domain (ECD) with three Ig-like domains, a 21 aa transmembrane segment, and a 411 aa cytoplasmic domain that contains the tyrosine kinase domain (2). Alternative splicing generates an additional isoform (IIIb) with a substitution in the third Ig-like domain (3). Within the ECD, mouse FGF R3 (IIIb) shares 91% and 98% aa sequence identity with comparable isoforms of human and rat FGF R3, respectively. The FGF R3 (IIIb) triggers cell proliferation in response to FGF acidic and FGF-9, while FGF R3 (IIIc) shows a wider selectivity that includes FGF acidic, FGF basic, FGF-4, -8, -9, -17, -18, -19, and -20 (4, 5). Ligand binding induces receptor dimerization and acitvation of the tyrosine kinase domain (1). FGF mediated activation of FGF R3 is dependent on the presence of heparan sulfate proteoglycans (6). FGF R3 functions as a negative regulator of endochondral bone growth, and FGF R3 mutations are associated with chondrodysplasia in humans (7, 8). In addition, the development of many cancers is associated with mutations or dysregulation of FGF R3 which can result in constitutive receptor activation (1).
  1. Turner, N. and R. Grose (2010) Nat. Rev. Cancer 10:116.
  2. Katoh, O. et al. (1993) Cancer Res. 53:1136.
  3. Chellaiah, A.T. et al. (1994) J. Biol. Chem. 269:11620.
  4. Ornitz, D.M. et al. (1996) J. Biol. Chem. 271:15292.
  5. Zhang, X. et al. (2006) J. Biol. Chem. 281:15694.
  6. Ornitz, D.M. and P. Leder (1992) J. Biol. Chem. 267:16305.
  7. Deng, C. et al. (1996) Cell 84:911.
  8. Colvin, J.S. et al. (1996) Nat. Genet. 12:390.

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Bioinformatics

Gene Symbol Fgfr3
Uniprot