Recombinant Human FGFR4 Fc Chimera Protein, CF

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Recombinant Human FGFR4 Fc Chimera Protein, CF Summary

Product Specifications

>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.
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.
Mouse myeloma cell line, NS0-derived human FGFR4 protein
Human FGF R4
Accession # P22455
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
65 kDa (monomer)
100-110 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


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.
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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).

  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
Entrez Gene IDs
2264 (Human); 14186 (Mouse)
Alternate Names
CD334 antigen; CD334; EC 2.7.10; EC; 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

Citations for Recombinant Human FGFR4 Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

5 Citations: Showing 1 - 5
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  1. FGF21-FGFR4 signaling in cardiac myocytes promotes concentric cardiac hypertrophy in mouse models of diabetes
    Authors: C Yanucil, D Kentrup, X Li, A Grabner, K Schramm, EC Martinez, J Li, I Campos, B Czaya, K Heitman, D Westbrook, AR Wende, A Sloan, JM Roche, A Fornoni, MS Kapiloff, C Faul
    Scientific Reports, 2022-05-05;12(1):7326.
    Species: Human
    Sample Types: Recombinant Proteins
    Applications: Bioassay
  2. Pre-clinical development of U3-1784, a novel FGFR4 antibody against cancer, and avoidance of its on-target toxicity
    Authors: R Bartz, K Fukuchi, T Ohtsuka, T Lange, K Gruner, I Watanabe, S Hayashi, Y Oda, R Kawaida, H Komori, Y Kashimoto, P Wirtz, JA Mayer, M Redondo-Mü, S Saito, M Takahashi, H Hanzawa, E Imai, A Martinez, M Hanai, D Häussinger, RW Chapman, T Agatsuma, J Bange, R Abraham
    Mol. Cancer Ther., 2019-07-26;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: ELISA Capture
  3. Molecular elements in FGF19 and FGF21 defining KLB/FGFR activity and specificity
    Authors: A Agrawal, S Parlee, D Perez-Tilv, P Li, J Pan, PA Mroz, AM Kruse Hans, B Andersen, B Finan, A Kharitonen, RD DiMarchi
    Mol Metab, 2018-05-11;13(0):45-55.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  4. Retinoic acid signalling specifies intermediate character in the developing telencephalon.
    Authors: Marklund M, Sjodal M, Beehler BC, Jessell TM, Edlund T, Gunhaga L
    Development, 2004-08-04;131(17):4323-32.
    Species: Chicken
    Sample Types: Whole Tissue
    Applications: Bioassay
  5. Specification of dorsal telencephalic character by sequential Wnt and FGF signaling.
    Authors: Gunhaga L, Marklund M, Sjodal M, Hsieh JC, Jessell TM, Edlund T
    Nat. Neurosci., 2003-07-01;6(7):701-7.
    Species: Chicken
    Sample Types: Whole Tissue
    Applications: Bioassay


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