Recombinant Human Fibroblast growth factor 2 (FGF2), partial (Active)

FGF2 drives proliferation, angiogenesis, and pluripotency maintenance through FGFR activation, making validated potency critical for reproducible downstream results. This tag-free recombinant human FGF2 (residues 132–288 of Isoform 1), covering the mature mitogenic domain, demonstrates an ED50 of 1.11 ng/mL in BALB/c 3T3 proliferation assays—confirming receptor-binding potency suitable for stem cell maintenance cultures, neuronal differentiation protocols, and angiogenesis models. Expression in *E. coli* is appropriate here because native FGF2 is non-glycosylated, ensuring that the recombinant form retains full biological equivalence to the endogenous ligand without post-translational modification concerns. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the criteria typical for cell-based proliferation and survival assays, receptor-ligand binding studies by SPR or ELISA, and in vivo wound healing or tumor biology experiments where endotoxin contamination would confound results.