Recombinant Human FGFR4 Fc Chimera Avi-tag Protein, CF

In a Human FGF acidic/FGF1 antibody (AF232) coated plate, in the presence of 50.0 ng/mL of Recombinant Human FGF acidic/FGF1 (232-FA), Biotinylated Recombinant Human FGFR4 Fc Chimera Avi-tag Protein (Catalog # AVI685) binds with an ED50 of 50.0-400 ng/mL.

2 μg/lane of Biotinylated Recombinant Human FGFR4 Fc Chimera Avi-tag Protein (Catalog # AVI685) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 90-105 kDa and 180-210 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human FGFR4 Fc Chimera 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 FGFR4 Fc Chimera Avi-tag Protein binds with an ED₅₀ of 50.0‑400 μg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human FGFR4 protein
  

  Human FGFR4 (Leu22-Asp369) Accession # P22455.2	IEGRMD	Human IgG1 Fc (Pro100-Lys330)	Avi-tag
  N-terminus			C-terminus

• Accession #: P22455.2
• N-terminal Sequence: Leu22
• 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: 67 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: 90-105 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 FGFR4 Fc Chimera Avi-tag Protein, CF

• CD334 antigen
• CD334
• EC 2.7.10
• EC 2.7.10.1
• FGF R4
• FGFR4
• FGFR-4
• fibroblast growth factor receptor 4
• JTK2hydroxyaryl-protein kinase
• MGC20292
• protein-tyrosine kinase
• TKF
• tyrosine kinase related to fibroblast growth factor receptor
• tyrosylprotein kinase

Background

Fibroblast growth factor receptor 4 (FGFR4) 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 human FGFR4 shares 90% amino acid sequence identity with mouse FGFR4. Alternative splicing of the IgIII domain generates multiple forms of FGFR13, but FGFR4 does not have a splice variant (3, 4). FGFR4 exhibits distinct and varying binding affinities for different FGF ligands, with FGF1, FGF4, and FGF8 showing the highest affinity (4). 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). FGFR4 is expressed at high levels during embryonic development and is required for the maintenance of both lipid and glucose metabolism as well as an established role in cholesterol metabolism (7). Overexpression of the FGFR4 has been reported in several solid tumors including breast cancer, prostate cancer, pancreatic cancer, and renal cell carcinoma (4, 8). Further, FGFR4 expression is significantly upregulated in most liver cancer cases, and enhanced FGF19-FGFR4 signaling is linked to hepatocellular carcinoma progression, metastasis, and poor survival (8). FGFR4 is being explored as a potential therapeutic target for breast cancer and other solid tumors (9). Our Avi-tag Biotinylated FGFR4 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. Lang, L. and Teng, Y. (2019) Cells. 8:31.
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. Huang, X. et al. (2007) Diabetes 56:2501.
8. Liu, Y. et al. (2020) Front Cell Dev Biol. 8:95.
9. Levine, K.M. et al. (2020) Pharmacol Ther. 214:107590.

Bioinformatics

• Uniprot:
  • P22455.2()