Recombinant Human FGFR3 alpha (IIIb) Fc Avi-tag Protein, CF Summary
|Human FGFR3 alpha (IIIB)|
Accession # NP_001156685.1
|IEGRMD||Human IgG1 Fc|
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Biotinylated Recombinant Human FGFR3 (IIIb) Fc Chimera Avi-tag Protein (Catalog # AVI11029) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 92-104 kDa and 184-208 kDa, respectively.
Fibroblast growth factor receptor 1 (FGFR1) belongs to a family of type I transmembrane tyrosine kinases which mediate the biological functions of FGFs that are involved in a multitude of physiological and pathological cellular processes (1). The FGFR family is comprised of 4 structurally conserved members (FGFR1-4) all possessing and extracellular domain (ECD) with three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain (1, 2). The ECD of mature, full-length FGFR3 shares 92% amino acid sequence identity with mouse FGFR3. Alternative splicing generates multiple forms of FGFR1-3, each with unique signaling characteristics (1-3). For FGFR3, alternative splicing of the ECD, specifically the IgIII domain, results in IIIb, or IIIc isoforms (4). The FGFR splice variants also exhibit distinct and varying binding affinities for different FGF ligands (2). FGFRs mediate the FGF signaling cascade which regulate developmental processes including cellular proliferation, differentiation, and migration, morphogenesis, and patterning (5). FGFRs transduce the signals through three dominant pathways including RAS/MAPK, PI3k/AKT, and PLC gamma (6). FGFR3 is normally expressed in the tissues of the central nervous system, brain, kidney and testis, with the FGFR3A(IIIb) splice variant predominantly expressed in epithelial cells (7, 8). FGFR3 signaling is critical for bone growth regulation and mutations in FGFR3 or misregulation of FGFR3 mediated signaling is found in multiple skeletal dysplasias, with FGFR3A(IIIb) specifically upregulated in hepatocellular carcinoma but down regulated in colorectal cancer (1,4, 8, 9). Our Avi-tag Biotinylated FGFR3A(IIIb) features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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- Ferguson, H.R. et al. (2021) Signaling. Cells 10:1201.
- Holzmann, K. et al. (2012) J Nucleic Acids. 2012:950508.
- Xie, Y. et al. (2020) Sig Transduct Target Ther 5:181.
- Mossahebi-Mohammadi, M. et al. (2020) Front Cell Dev Biol. 18:79.
- Sturla, L.M. et al. (2003) Br. J. Cancer 89:1276.
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- Teven, C.M. et al. (2014) Genes Dis. 1:199.
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