FGF1 Knockout Cell Line (HEK 293)

The choice depends on whether you are studying FGF1 (fibroblast growth factor 1, acidic FGF)'s role as a pan-FGFR-activating growth factor or its emerging functions in metabolic disease therapy. The Knockout line is the standard tool for asking whether FGF1 is required for autocrine FGFR signaling — FGF1 is unique among FGFs in binding all four FGFR receptors (FGFR1-4) with high affinity, making it a 'universal' FGF ligand; FGF1 has emerged as a glucose-lowering hormone with insulin-like effects, attracting interest for diabetes therapeutic development. Overexpression is useful for studying FGF1 gain-of-function effects. For FGF-FGFR signaling research, the EDITGENE FGF1 Knockout in HEK293 enables study of autocrine FGF1 production. Rescue with wild-type or receptor-binding-deficient FGF1 enables structure-function studies. The knockout is valuable for studying FGF1-mediated metabolic effects, FGFR pan-activation biology, and emerging FGF1-based diabetes therapeutics (engineered FGF1 variants with reduced mitogenic activity but retained glucose-lowering).

Primary applications: • FGF1 secretion: secreted FGF1 quantification by ELISA — FGF1 is a non-classical secretion pathway protein (lacks signal peptide; secreted via copper-mediated translocation across the plasma membrane under cellular stress). • Autocrine FGFR signaling: phospho-FRS2, phospho-MAPK, phospho-AKT analysis in FGF1-null cells with FGFR-expressing background. • Metabolic studies: insulin sensitivity and glucose uptake assays given FGF1's emerging glucose-lowering activity. • Engineered FGF1 variants: rescue with FGF1ΔHBS (heparin-binding-site mutant) or non-mitogenic engineered variants for emerging FGF1-based diabetes therapeutic studies. EDITGENE recommends this model for researchers investigating FGF1 biology, FGFR pan-activation, and emerging FGF1-based metabolic disease therapeutics.

Yes. FGF1 rescue experiments require attention to non-classical secretion: • Construct design: use a codon-modified FGF1 sequence with a small N-terminal tag (FLAG, HA) — FGF1 lacks a signal peptide and is secreted via a non-classical copper-mediated pathway under cellular stress; tag placement requires care. • Secretion validation: confirm conditioned media FGF1 levels by ELISA — FGF1 secretion is stress-induced (heat shock, hypoxia, serum starvation). • Heparin-binding-deficient rescue: FGF1ΔHBS (K127D/R133E/K134Q) abolishes heparin/HSPG binding but retains FGFR binding — useful for engineered FGF1 variants. • Non-mitogenic rescue: engineered FGF1 variants with reduced mitogenic activity but retained glucose-lowering enable separation of metabolic from proliferative effects. • Functional readout: rescue should restore conditioned-media FGF1 levels and autocrine FGFR activation. HEK293 transduces efficiently with lentivirus and supports stable rescue line generation.