Recombinant Human FGFR2 alpha (IIIc) His Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein
(Catalog #
232-FA/CF) is in the presence at 50.0 ng/mL (100 μL/well), Biotinylated Recombinant Human FGFR2 alpha (IIIc) His-tag Avi-tag binds with an ED 50 of 0.300-3.00 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human FGFR2 alpha protein Human FGFR2 alpha (IIIc) (Arg22-Glu377) Accession # P21802.1 | 6-His tag | Avi-tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Arg22 |
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
Theoretical MW |
40 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 |
68-78 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 FGFR2 alpha (IIIc) His Avi-tag Protein, CF
Background
Fibroblast
growth factor receptor 2 (FGFR2) 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 an 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 cytoplasmic split tyrosine-kinase domain (1, 2). The ECD of
mature, full-length FGFR2 shares 95% amino acid sequence identity with mouse
FGFR2. Alternative splicing generates multiple forms of FGFR1-3, each with
unique signaling characteristics (1-3). For FGFR2, 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, 4). Specifically, FGFR2A (IIIc) binds most FGF ligands
but not the FGF10 subfamily, while FGFR2A (IIIc) binds only members of the FGF10 subfamily (5). FGFRs mediate
the FGF signaling cascade which regulate developmental processes including
cellular proliferation, differentiation, and migration, morphogenesis, and
patterning (6). FGFRs transduce the signals through three dominant pathways
including RAS/MAPK, PI3k/AKT, and PLC gamma (7). While FGFR2 is widely expressed in
many adult human tissues, isoform expression is tissue specific, with IIIb predominantly expressed in epithelial cells, while IIIc
is expressed in mesenchymal cells (5). FGFR2 signaling is critical for embryonic development, tissue repair, and regulation
of osteoblast function and bone growth (8). Mutations in FGFR2 or
misregulation of FGFR2 mediated signaling is found in multiple skeletal
dysplasias, with FGFR2A (IIIc) specifically
upregulated in several cancers including prostate, breast and pancreatic and is
proposed as a novel therapeutic target for colorectal carcinomas (6, 9). Our Avi-tag Biotinylated FGFR2 protein 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.
- Wagner, E.J. et al. (2003) RNA 9:1552.
- Xie, Y. et al. (2020) Sig Transduct Target Ther 5:181.
- Mossahebi-Mohammadi, M. et al. (2020) Front Cell Dev Biol. 18:79.
- Teven, C.M. et al. (2014) Genes Dis. 1:199.
- Matsuda, Y. et al. (2012) Mol Cancer Ther. 11:2010.
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