Recombinant Human FGFR1 alpha (IIIc) Fc Avi-tag Protein, CF

Recombinant Human FGFR1 alpha (IIIc) Fc 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: FGFR1 alpha

Fibroblast growth factor receptor 1 (FGFR1) 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 an 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, full-length FGFR1 shares 98% amino acid sequence identity with mouse FGFR1. Alternative splicing generates multiple forms of FGFR1-3, each with unique signaling characteristics (3). For FGFR1, alternative splicing of the ECD generates FGFR1A, FGFR1B, and FGFR1G isoforms of the receptor with the A isoform containing three Ig domains, while the B and G isoforms lack the N-terminal IgI domain (3). Additional splicing of the IgIII domain, results in IIIa, IIIb, or IIIc isoforms (3). Only the alpha isoform has been identified for FGFR3 and FGFR4 and FGFR4 also lacks the IIIb and IIIc splicing events (4). The FGFR splice variants also exhibit distinct and varying binding affinities for different FGF ligands (2). 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). FGFR1 the most abundant FGFR and is widely expressed in many adult human tissues, but the splice variants display distinct tissue-specific differences with IIIc splice variants expressed in mesenchymal tissue (4, 7, 8). Mutations in FGFR1 or misregulation of FGFR1 mediated signaling is found in multiple diseases, with FGFR1A(IIIc) specifically upregulated, from breast and pancreatic cancer to Pfeiffer syndrome and osteoarthritis (4, 9-11). A soluble version of the FGFR1A(IIIc) splice variant has shown anti- angiogenic and anti-proliferative properties in multiple cancer cell line models (11). Our Avi-tag Biotinylated FGFR1A(IIIc) 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

• Cytokine and Growth Factor Receptors on VSMC
• FGF Family
• FGF Ligands
• FGF Regulators
• Glial Lineage Markers
• Receptor Tyrosine Kinases (RTKs)
• Receptor Tyrosine Kinases (RTKs) in the Akt Pathway
• Receptors in the Jak/STAT Pathway