Recombinant Mouse FGFR4 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse FGFR4 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit FGF acidic-dependent proliferation of NR6R‑3T3 mouse fibroblast cells. The ED50 for this effect is typically 7-35 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse FGF R4 protein
Mouse FGF R4
(Leu19-Asp366)
Accession # Q03142
IEGRMDP Mouse IgG2A
(Glu98-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Leu19
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Fgfr4
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
66 kDa (monomer).
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
90-100 kDa, reducing conditions
Publications
Read Publication using
2265-FR in the following applications:

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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 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 Mouse FGFR4 Fc Chimera 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 (FGF R4), also known as CD334, is a 110 kDa glycosylated transmembrane receptor tyrosine kinase (1). Mature mouse FGF R4 consists of a 350 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, mouse FGF R4 shares 90% and 96% aa sequence identity with human and rat FGF R4, respectively. Alternate splicing generates additional isoforms that have deletions within or C-terminal to the kinase domain (3, 4). FGF R4 is widely expressed during embryonic development and in adult liver, kidney, and lung (2, 5, 6, 7). It binds FGF acidic, FGF basic, FGF-8, -15, and -19 (6, 8‑12). 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 (7, 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 (7, 11). FGF R4 signaling is additionally required for skeletal muscle development in limbs (4, 6). FGF R4 interacts in cis with cell surface MMP-14, leading to down‑regulation of both proteins (14). In contrast, the Arg388 variant of FGF R4, which is associated with tumor progression in human cancer, is activated and stabilized by MMP-14 (14, 15).
  1. Haugsten, E.M. et al. (2010) Mol. Cancer Res. 8:1439.
  2. Stark, K.L. et al. (1991) Development 113:641.
  3. van Heumen, W.R.A. et al. (1999) IUBMB Life 48:73.
  4. Kwiatkowski, B.A. et al. (2008) J. Cell Physiol. 215:803.
  5. Korhonen, J. et al. (1992) Int. J. Dev. Biol. 36:323.
  6. Marics, I. et al. (2002) Development 129:4559.
  7. Luo, Y. et al. (2010) J. Biol. Chem. 285:30069.
  8. Partanen, J. et al. (1991) EMBO J. 10:1347.
  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. Sugiyama, N. et al. (2010) Proc. Natl. Acad. Sci. 107:15786.
  15. Bange, J. et al. (2002) Cancer Res. 62:840.

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Publications for FGFR4 (2265-FR)(1)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 1 application: ELISA Capture.


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Bioinformatics

Gene Symbol Fgfr4
Uniprot