FGFR4 Reporter Assay System (human)

This is an all-inclusive cell-based luciferase reporter assay kit targeting the Human Fibroblast Growth Factor Receptor 4 (FGFR4). INDIGO's FGFR4 reporter assay utilizes proprietary mammalian cells that have been engineered to provide constitutive expression of the Human Fibroblast Growth Factor Receptor 4. In addition to FGFR4 Reporter Cells, this kit provides two optimized media for use during cell culture and in diluting the user's test samples, a reference agonist, Luciferase Detection Reagent, and a cell culture-ready assay plate. The principal application of this assay is in the screening of test samples to quantify any functional activity, either agonist or antagonist, that they may exert against human FGFR4. This kit provides researchers with clear, reproducible results, exceptional cell viability post-thaw, and consistent results lot to lot. Kits must be stored at -80C. Do not store in liquid nitrogen. Note: reporter cells cannot be refrozen or maintained in extended culture. Features Ready to Use Upon Receipt Includes All Needed Components Contains Transfected Reporter Cells Eliminates Cell Licensing Fees Clear, Reproducible Results Consistent Results Lot to Lot Product Specifications Target Type Growth Factor Receptor Species Human Receptor Form Hybrid Assay Mode Agonist, Antagonist Kit Components FGFR4 Reporter Cells Cell Recovery Medium (CRM) Compound Screening Medium (CSM) FGF-2, (ref. activator, in PBS/0.1% BSA ) Detection Substrate Detection Buffer White, sterile, cell-culture ready assay plate Shelf Life 6 months Shipping Requirements Dry Ice Storage temperature -80C. Target Background The family of Fibroblast Growth Factors (FGFs) comprise approximately 23 members that are related by core sequence and structure conservation, with the majority of FGFs being secreted signaling proteins. Secreted FGFs are predominantly autocrine and paracrine factors, with only three members evolved to function as endocrine factors. FGFs bind and activate four FGF Receptors (FGFR1-4) which, themselves, are members of the family of high-affinity tyrosine kinase receptors. Heparin and heparin sulfate proteoglycans (HSPGs) are essential cofactors for paracrine FGF (e.g., FGF-1 and FGF-2) interactions with FGFRs. The association between paracrine FGFs and HSPGs ensures their limited diffusion and enhanced FGFR binding specificity. In contrast to the paracrine ligand activators of FGFR, endocrine FGFs (e.g., FGF-19, FGF-21, and FGF-23) have minimal affinity to heparin. Rather, they typically require association with members of the Klotho family of proteins as cofactors for efficient binding to their cognate receptor(s). Although, FGF-23 activation of FGFR3 can occur in a Klotho independent manner, signaling through the PLCgamma/calcineurin/NFAT pathway. The FGFs are broad-spectrum mitogens that, through their receptor interactions, regulate a variety of cellular functions including migration, proliferation, differentiation, metabolism and survival. In particular, FGF/FGFR signaling plays a critical role in regulating metabolism in the kidney, liver, brain, intestine and adipose tissues. Not surprisingly, dysfunctional FGFR signaling can lead to a range of physiological disorders. For example, mutation, amplification, and gene fusion may result in abnormal morphogenesis and the progression of several types of cancer. Consequently, the FGF receptors continue to command much interest as targets for drug development and drug safety screening.