Recombinant Human FGF acidic is a single, non-glycosylated polypeptide chain containing 141 amino acids.
Background: Fibroblast Growth Factor acidic (FGF acidic), also known as FGF-1 and endothelial cell growth factor, is a member of the fibroblast growth factor (FGF) family. Fibroblast growth factor was found in pituitary extracts in 1973 and then tested in a bioassay that caused fibroblasts to proliferate. After further fractionating the extract using acidic and basic pH, two different forms have isolated that named “acidic fibroblast growth factor" (FGF1) and “basic fibroblast growth factor” (FGF2). Human FGF-acidic shares 54% amino acid sequence identity with FGF-basic. In mammalian FGF receptor family has 4 members, FGFR1, FGFR1, FGFR3, and FGFR4, and 1, 2, 3 have 2 sub-types “b”, “c”. aFGF can bind and activate all 7 different FGFRs. Affinity between aFGF and its receptors can be increased by heparin or heparin sulfate proteoglycan. FGF-acidic plays an important role in the regulation of cell survival, cell division, antiogenesis, cell differentiation and cell migration. FGF-acidic is also involved in a variety of biological processes, including embryonic development, morphogenesis, tissue repair, tumor growth and invasion.