Recombinant Mouse FGFR2 alpha (IIIb) Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. 200 ng/mL of biotinylated rmFGF1 is mixed with serially diluted rmFGF R2 alpha (IIIb)/Fc. Following incubation, the FGF R2 alpha (IIIb)/Fc-FGF1/biotin complex is captured on an EvenCoatTM Streptavidin Microplate (Catalog # CP003). Bound FGF R2 alpha (IIIb)/Fc is measured using HRP labeled Gt x Human IgG Fc. The concentration of rmFGF R2 alpha (IIIb)/Fc Chimera that produces 50% of the optimal binding was found to be approximately 150‑600 ng/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse FGF R2 alpha protein
Mouse FGF R2a (IIIb) (Arg22 - Glu378) (Asn314His) Accession # ABL89196 |
IEGRMD |
Human IgG1 (Pro100 - Lys330) |
N-terminus |
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Arg22, Ser24, and Leu27 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Fgfr2 |
Purity |
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
66.2 kDa (monomer). 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 |
105-120 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 |
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 100 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 FGFR2 alpha (IIIb) Fc Chimera Protein, CF
Background
Fibroblast growth factor receptor 2 alpha (FGF R2 alpha ) is a 140 kDa type I transmembrane receptor tyrosine kinase that mediates the heparan sulfate proteoglycan-dependent biological activity of several FGFs. It is a member of the FGF R family of proteins whose extracellular domains (ECD) contain three immunoglobulin (Ig)-like domains with a series of acidic residues between the first and second Ig-like domains (1, 2). Multiple forms of FGF R2 are generated by alternative splicing (1, 2). Alpha isoforms contain all three Ig-like domains, while beta forms lack the first Ig-like domain (3, 4). The C-terminal portion of the third Ig-like domain can be encoded by either of two mutually exclusive exons, giving rise to the IIIb/KGFR and IIIc/BEK isoforms with distinct ligand selectivity (3, 4). This recombinant protein corresponds to the ECD from Accession # ABL89196. It shares 94% amino acid sequence identity with the ECD of human FGF R2 alpha (IIIb). FGF R2 alpha (IIIb) signals in response to FGF-1, -3, -7, -10, and -22, leading to receptor dimerization and autophosphorylation of its tyrosine kinase domain (1, 2, 5, 6). In contrast, the IIIc isoform preferentially responds to FGF-1, -2, -4, -5, -6, -8, -9, -16, -17, -18, and -20 (5, 6). FGF R2 alpha (IIIb) is widely expressed on epithelial cells, while its ligands are typically expressed by neighboring mesenchymal cells (2, 7). Its involvement in epithelial-mesenchymal interactions plays an important role in the morphogenesis of many tissues. Knockout mice exhibit widespread developmental defects due to an unresponsiveness to normal mitogenic stimulation (8 - 11). Mutations in FGF R2 alpha (IIIb) as well as altered splicing patterns (to isoform IIIc) are associated with a variety of skin and skeletal disorders and the progression of many epithelial cancers (12 - 14).
- Wiedlocha, A. and V. Sorensen (2004) Curr. Topics Microbiol. Immunol. 286:45.
- Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
- Miki, T. et al. (1991) Science 251:72.
- Mansukhani, A. et al. (1992) Proc. Natl. Acad. Sci. 89:3305.
- Ornitz, D.M. et al. (1996) J. Biol. Chem. 271:15292.
- Zhang, X. et al. (2006) J. Biol. Chem. 281:15694.
- Finch, P.W. et al. (1995) Dev. Dyn. 203:223.
- Petiot, A. et al. (2003) Development 130:5493.
- Marguerie, A. et al. (2006) Cardiovasc. Res. 71:50.
- Revest, J.-M. et al. (2001) Dev. Biol. 231:47.
- Petiot, A. et al. (2005) Development 132:2441.
- Katoh, M. (2009) J. Invest. Dermatol. 129:1861.
- Su, N. et al. (2008) Front. Biosci. 13:2842.
- Acevedo, V.D. et al. (2009) Cell Cycle 8:580.
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