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Recombinant Human FGFR5/FGFRL1 Protein, CF

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Recombinant Human FGF R5/FGFRL1 (Catalog # 9805-FR) supports MG-63human bone Fibroblasts adhesion. The ED50 for this effect is 1.5‑7.5 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human FGFR5/FGFRL1 Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of MG-63 human bone fibroblasts. The ED50 for this effect is 1.5-7.5 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human FGF R5/FGFRL1 protein
Ala25-Pro378, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ala25
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
40 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
54-63 kDa, 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.
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 FGFR5/FGFRL1 Protein, CF

  • FGF homologous factor receptor
  • FGF R5
  • FGF receptor-like protein 1
  • FGFR5
  • FGFR-5
  • FGFRL1
  • FGFR-like protein
  • FHFR
  • Fibroblast growth factor receptor 5
  • fibroblast growth factor receptor-like 1

Background

Fibroblast growth factor receptor 5 (FGF R5), also known as FGRL1, is a 65 kDa transmembrane member of the FGF receptor family (1). Mature mouse FGF R5 consists of a 354 amino acid (aa) extracellular domain (ECD) with three immunoglobulin-like domains, a 21 aa transmembrane segment, and a 134 aa cytoplasmic domain (2). FGF R5 is distinct from other FGF receptor family members in that it does not contain a cytoplasmic tyrosine kinase domain (2, 3). Within the ECD, mouse FGF R5 shares 94% and 98% aa sequence identity with human and rat FGF R5, respectively. Alternate splicing results in an isoform that lacks the first Ig-like domain (2). FGF R5 is widely expressed, and expression of two species of mRNA in cartilage and pancreas may indicate the presence of both splice forms (2-6). Both the full length and truncated isoforms of FGF R5 bind FGF basic; the full length form additionally binds to heparin (2, 6). FGF R5 may function as a decoy receptor by binding FGF but not transducing its mitogenic signals (6). FGF R5 is found in most multicellular animals. It is known to bind to FGF ligands, with high affinity to FGF-3, -4, -8, -10, and -22 and weaker affinity to FGF-2, -5, -17, -18 and -23 (7). The extracellular domain of FGF R5 promotes cell adhesion when mediated by heparin sulfate glycosaminoglycans on the cell surface (8, 9). Comparing to the signaling receptors of FGFR family members (FGF R1-FGF R4), FGF R5 is more similar to the nectins for its adhesion properties and has no effect on cell growth and proliferation (9).
  1. Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
  2. Sleeman, M. et al. (2001) Gene 271:171.
  3. Kim, I. et al. (2001) Biochim. Biophys. Acta 1518:152.
  4. Antoine, M. et al. (2005) Growth Factors 23:87.
  5. Wiedemann, M. et al. (2000) Genomics 69:275.
  6. Trueb, B. et al. (2003) J. Biol. Chem. 278:33857.
  7. Steinberg, F. et al (2010). J Biol Chem 285:2193.
  8. Rieckmann, T. et al (2008) Exp Cell Res 314:1071.
  9. Yang, X. et al (2016) International J Molec Med. 38:30.

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