Recombinant Human FGFR4 Fc Chimera Avi-tag Protein, CF

Recombinant Human FGFR4 Fc Chimera Avi-tag Protein, CF Summary

Product Specifications

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.

Background: FGFR4

Fibroblast growth factor receptor 4 (FGFR4) belongs to a family of type I transmembrane tyrosine kinases which mediate the biological functions of FGFs that are involved in a multitude of physiological and pathological cellular processes (1). The FGFR family is comprised of 4 structurally conserved members (FGFR1-4) all possessing and extracellular domain (ECD) with three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain (1, 2). The ECD of mature human FGFR4 shares 90% amino acid sequence identity with mouse FGFR4. Alternative splicing of the IgIII domain generates multiple forms of FGFR13, but FGFR4 does not have a splice variant (3, 4). FGFR4 exhibits distinct and varying binding affinities for different FGF ligands, with FGF1, FGF4, and FGF8 showing the highest affinity (4). FGFRs mediate the FGF signaling cascade which regulate developmental processes including cellular proliferation, differentiation, and migration, morphogenesis, and patterning (5). FGFRs transduce the signals through three dominant pathways including RAS/MAPK, PI3k/AKT, and PLC gamma (6). FGFR4 is expressed at high levels during embryonic development and is required for the maintenance of both lipid and glucose metabolism as well as an established role in cholesterol metabolism (7). Overexpression of the FGFR4 has been reported in several solid tumors including breast cancer, prostate cancer, pancreatic cancer, and renal cell carcinoma (4, 8). Further, FGFR4 expression is significantly upregulated in most liver cancer cases, and enhanced FGF19-FGFR4 signaling is linked to hepatocellular carcinoma progression, metastasis, and poor survival (8). FGFR4 is being explored as a potential therapeutic target for breast cancer and other solid tumors (9). Our Avi-tag Biotinylated FGFR4 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

Related Research Areas

• Cancer Biomarkers
• FGF Family
• FGF Ligands
• FGF Regulators
• Glial Lineage Markers
• Neural Stem Cell Markers
• Receptor Tyrosine Kinases (RTKs)
• Receptor Tyrosine Kinases (RTKs) in the Akt Pathway
• Receptors in the Jak/STAT Pathway