Recombinant Human FGFR1 alpha (IIIc) Fc Avi-tag Protein, CF

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In a Human FGFacidic/FGF1 antibody (AF232) coated plate, in the presence of 50 ng/mL of Recombinant Human FGFacidic/FGF1 (232-FA), Recombinant Human FGFR1 alpha (IIIc) Fc Avi-tag Protein (Catalog # AVI11031) binds with ...read more
2 μg/lane of Biotinylated Recombinant Human FGFR1 alpha (IIIc) Fc Chimera Avi-tag Protein (Catalog # AVI11031) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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 ED50 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
IEGRDMDHuman IgG1
(Pro100-Lys330)
Avi-tag
N-terminusC-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
  • Bioactivity
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

  • FGF R1a
  • FGFR1 alpha

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.
  1. Ornitz, D.M. and Itoh, N. (2015) Wiley Interdiscip Rev Dev Biol. 4:215.
  2. Zhang, X. et al. (2006) J Biol Chem. 281:15694.
  3. Ferguson, H.R. et al. (2021) Signaling. Cells 10:1201.
  4. Holzmann, K. et al. (2012) J. Nucleic. Acids. 2012:950508.
  5. Xie, Y. et al. (2020) Sig Transduct Target Ther. 5:181.
  6. Mossahebi-Mohammadi, M. et al. (2020) Front Cell Dev. Biol. 18:79.
  7. Hughes, S.E. (1997) J. Histochem Cytochem. 45:1005.
  8. Delezoide, A.L. et al. (1998) Mech Dev. 77:19.
  9. Yamashita-Sugahara, Y. et al. (2016) Sci Rep 6:35908.
  10. Teven, C.M. et al. (2014) Genes Dis. 1:199.
  11. Babina, I. and Turner, N. (2017) Nat. Rev. Cancer 17:318.

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