Recombinant Human FGFR1 alpha (IIIc) Fc 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, Biotinylated Recombinant Human FGFR1 alpha (IIIc) Fc Chimera Avi-tag Protein binds with an ED 50 of 0.100-0.600 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human FGFR1 alpha protein Human FGF R1 alpha (IIIc) (Arg22-Glu376) Accession # NP_075598.2 | IEGRDMD | Human IgG1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Arg22 |
Structure / Form |
Disulfide-linked homodimer 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 |
68 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 |
100-120 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 FGFR1 alpha (IIIc) Fc Avi-tag Protein, CF
Background
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 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 the split tyrosine-kinase domain (1, 2). The ECD of
mature, full-length FGFR1 shares 98% amino acid sequence identity with mouse
FGFR1. Alternative splicing generates
multiple forms of FGFR1-3, each with unique signaling characteristics (3).
For FGFR1, alternative splicing of the ECD generates FGFR1A, FGFR1B, and FGFR1G
isoforms of the receptor with the A isoform containing three Ig domains, while
the B and G isoforms lack the N-terminal IgI domain (3). Additional splicing of
the IgIII domain, results in IIIa, IIIb, or IIIc isoforms (3). Only the alpha
isoform has been identified for FGFR3 and FGFR4 and FGFR4 also lacks the IIIb
and IIIc splicing events (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). FGFR1 the most abundant FGFR and is widely expressed in
many adult human tissues, but the splice variants display distinct
tissue-specific differences with IIIc splice variants expressed in mesenchymal
tissue (4, 7, 8). Mutations in FGFR1 or misregulation of FGFR1 mediated
signaling is found in multiple diseases, with FGFR1A(IIIc) specifically upregulated, from
breast and pancreatic cancer to Pfeiffer syndrome and osteoarthritis (4, 9-11).
A soluble version of the FGFR1A(IIIc) splice variant has shown anti- angiogenic
and anti-proliferative properties in multiple cancer cell line models (11). Our
Avi-tag Biotinylated FGFR1A(IIIc) 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.
- Hughes, S.E. (1997) J. Histochem Cytochem. 45:1005.
- Delezoide, A.L. et al. (1998) Mech Dev. 77:19.
- Yamashita-Sugahara, Y. et al. (2016) Sci Rep 6:35908.
- Teven, C.M. et al. (2014) Genes Dis. 1:199.
- Babina, I. and Turner, N. (2017) Nat. Rev. Cancer 17:318.
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