Recombinant Human FGFR3 (IIIb) His-tag Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. In a Human FGF acidic/FGF1 antibody
(Catalog #
AF232)
coated plate, in the presence of 50.0 ng/mL of Recombinant Human FGF acidic/FGF1
(Catalog #
232-FA),
Biotinylated Recombinant Human FGFR3 (IIIb) His-tag Avi-tag Protein binds with an ED 50 of 1.00-6.00 µg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human FGFR3 protein Human FGFR3 (IIIb) (Glu23-Gly377) Accession # NP_001156685.1 | 6-His tag | Avi-tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Glu23 |
Structure / Form |
Biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
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 |
41 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 |
55-75 kDa, under 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 with Trehalose. |
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 Human FGFR3 (IIIb) His-tag Avi-tag Protein, CF
Background
Fibroblast
growth factor receptor 3 (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.
- Ornitz, D.M. and Itoh, N. (2015) Wiley Interdiscip. Rev. Dev. Biol. 4:215.
- Zhang, X. et al. (2006) J Biol. Chem. 281:15694.
- 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.
- Paur, J. et al. (2015) Hepatology. 62:1767.
- Teven, C.M. et al. (2014) Genes Dis. 1:199.
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