Recombinant Human FGFR4 Fc Chimera Protein, CF

R&D Systems | Catalog # 685-FR

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Key Product Details

  • R&D Systems NS0-derived Recombinant Human FGFR4 Fc Chimera Protein (685-FR)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

NS0

Accession Number

P22455

Structure / Form

Disulfide-linked homodimer

Applications

Bioactivity
View all FGFR4 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human FGFR4 protein
Human FGF R4
(Leu22-Asp369)
Accession # P22455		 IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus

Purity

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Leu22

Predicted Molecular Mass

65 kDa (monomer)

SDS-PAGE

100-110 kDa, reducing conditions

Activity

Measured by its ability to inhibit FGF acidic-dependent proliferation of NR6R‑3T3 mouse fibroblast cells.
The ED50 for this effect is 2‑6 ng/mL.

Formulation, Preparation, and Storage

685-FR
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution

Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: FGFR4

Fibroblast growth factor receptor 4 (FGF R4), also known as CD334, is a 110 kDa glycosylated transmembrane receptor tyrosine kinase (1). Mature human FGF R4 consists of a 348 amino acid (aa) extracellular domain (ECD) with three Ig‑like domains, a 21 aa transmembrane segment, and a 412 aa cytoplasmic domain that contains the tyrosine kinase domain (2). Within the ECD, human FGF R4 shares 90% and 88% aa sequence identity with mouse and rat FGF R4, respectively. Alternate splicing generates a potentially secreted isoform with a substitution encompassing the transmembrane segment (3). A 65 kDa N‑terminally truncated isoform lacks the signal peptide and first two Ig‑like domains. This isoform is produced in human pituitary adenomas and is constitutively phosphorylated and oncogenic (4). FGF R4 is widely expressed during embryonic development and in adult liver, kidney, and lung (5‑8). It binds FGF acidic, FGF basic, FGF‑8, -15, and -19 (2, 7, 9‑12). FGF R4 associates with beta-Klotho and sulfated glycosaminoglycans, and these interactions increase the affinity of FGF R4 for its ligands as well as its signaling capacity (8, 9, 12). FGF-19 induced signaling through FGF R4 is important for the regulation of bile acid synthesis and lipid and glucose homeostasis (10, 13). FGF R4 supports glucose tolerance and insulin sensitivity and protects against hyperlipidemia (13). It is down‑regulated in the liver during fasting and is up‑regulated by insulin (10). It can exert either proliferative or apoptotic effects on hepatocytes (8, 11). FGF R4 signaling is additionally required for skeletal muscle development in limbs (7, 14). FGF R4 interacts in cis with cell surface MMP-14, leading to down‑regulation of both proteins (15). In contrast, the Arg388 variant of FGF R4, which is associated with tumor progression in human cancer, is activated and stabilized by MMP-14 (15, 16).

References

  1. Haugsten, E.M. et al. (2010) Mol. Cancer Res. 8:1439.
  2. Partanen, J. et al. (1991) EMBO J. 10:1347.
  3. Takaishi, S. et al. (2000) Biochem. Biophys. Res. Commun. 267:658.
  4. Ezzat, S. et al. (2002) J. Clin. Invest. 109:69.
  5. Stark, K.L. et al. (1991) Development 113:641.
  6. Korhonen, J. et al. (1992) Int. J. Dev. Biol. 36:323.
  7. Marics, I. et al. (2002) Development 129:4559.
  8. Luo, Y. et al. (2010) J. Biol. Chem. 285:30069.
  9. Saxena, K. et al. (2010) J. Biol. Chem. 285:26628.
  10. Shin, D.J. and T.F. Osborne (2009) J. Biol. Chem. 284:11110.
  11. Wu, X. et al. (2010) J. Biol. Chem. 285:5165.
  12. Nakamura, M. et al. (2011) J. Biol. Chem. 286:26418.
  13. Huang, X. et al. (2007) Diabetes 56:2501.
  14. Kwiatkowski, B.A. et al. (2008) J. Cell Physiol. 215:803.
  15. Sugiyama, N. et al. (2010) Proc. Natl. Acad. Sci. 107:15786.
  16. Bange, J. et al. (2002) Cancer Res. 62:840.

Long Name

Fibroblast Growth Factor Receptor 4

Alternate Names

CD334, FGF R4

Entrez Gene IDs

2264 (Human); 14186 (Mouse)

Gene Symbol

FGFR4

UniProt

P22455

Additional FGFR4 Products

Product Documents for Recombinant Human FGFR4 Fc Chimera Protein, CF

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Product Specific Notices for Recombinant Human FGFR4 Fc Chimera Protein, CF

For research use only

Citations for Recombinant Human FGFR4 Fc Chimera Protein, CF

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