Recombinant Human FGFR5/FGFRL1 Protein, CF Summary
Product Specifications
Ala25-Pro378, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
9805-FR
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in 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.
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Scientific Data
Recombinant Human FGF R5/FGFRL1 (Catalog # 9805-FR) supports MG-63 human bone Fibroblasts adhesion. The ED50 for this effect is 1.5-7.5 μg/mL.
Reconstitution Calculator
Background: FGFR5/FGFRL1
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).
- Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
- Sleeman, M. et al. (2001) Gene 271:171.
- Kim, I. et al. (2001) Biochim. Biophys. Acta 1518:152.
- Antoine, M. et al. (2005) Growth Factors 23:87.
- Wiedemann, M. et al. (2000) Genomics 69:275.
- Trueb, B. et al. (2003) J. Biol. Chem. 278:33857.
- Steinberg, F. et al (2010). J Biol Chem 285:2193.
- Rieckmann, T. et al (2008) Exp Cell Res 314:1071.
- Yang, X. et al (2016) International J Molec Med. 38:30.
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