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Recombinant Mouse FGFR5 Fc Chimera Protein, CF

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Recombinant Mouse FGF R5 Fc Chimera (Catalog # 1899-FR) binds biotinylated Recombinant Mouse FGF1. The concentration of Recombinant Mouse FGF R5 Fc Chimera that produces50% of the optimal binding response is 30-120 ng/mL.
Recombinant Mouse FGF R5 Fc Chimera (Catalog # 1899-FR) binds biotinylated Recombinant Mouse FGF1. The concentration of Recombinant Mouse FGF R5 Fc Chimera that produces50% of the optimal binding response is 30-120 ...read more

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse FGFR5 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA.

200 ng/mL of biotinylated Recombinant Mouse FGF1 is mixed with serially diluted Recombinant Mouse FGF R5 Fc Chimera. Following incubation, the FGF R5-FGF1/biotin complex is captured on an EvenCoatTM Streptavidin Microplate (Catalog # CP003). Bound FGF R5 is measured using Rt x mFGF R5 followed by HRP labeled Gt x Rat IgG. The concentration of Recombinant Mouse FGF R5 Fc Chimera that produces 50% of the optimal binding is 30-120 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse FGF R5/FGFRL1 protein
Mouse FGF R5
(Ala21-Pro374)
Accession # NP_473412		 PIEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Ala21
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Fgfrl1
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
65.6 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
85-95 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
>90%, 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 FGFR5 Fc Chimera 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).
  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.

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Bioinformatics

Gene Symbol Fgfrl1
Uniprot