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 |
|
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
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).
- Turner, N. and R. Grose (2010) Nat. Rev. Cancer 10:116.
- Katoh, O. et al. (1993) Cancer Res. 53:1136.
- Chellaiah, A.T. et al. (1994) J. Biol. Chem. 269:11620.
- Ornitz, D.M. et al. (1996) J. Biol. Chem. 271:15292.
- Zhang, X. et al. (2006) J. Biol. Chem. 281:15694.
- Ornitz, D.M. and P. Leder (1992) J. Biol. Chem. 267:16305.
- Deng, C. et al. (1996) Cell 84:911.
- Colvin, J.S. et al. (1996) Nat. Genet. 12:390.
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