Skin Care aFGF EGF Recombinant Human Protein Human Fibroblast Growth Factor-Acidic rh-aFGF

FGF1, also known as acidic fibroblast growth factor (aFGF), is a growth factor and

signaling protein encoded by the FGF1 gene. It is synthesized as a 155 amino

acid polypeptide, whose mature form is a non-glycosylated protein.

Fibroblast growth factor protein was first purified in 1975, but soon afterwards

others using different conditions isolated acidic FGF, Heparin-binding growth

factor-1, and Endothelial cell growth factor-1. Gene sequencing revealed that this

group was actually the same growth factor and that FGF1 was a member of a family

of FGF proteins.

FGF-1 has no definitive signal sequence and thus is not secreted through classical

pathways, but it does appear to form a disulfide linked dimer inside cells that

associate with a complex of proteins at the cell membrane (including S100A13 and

Syt1) which then help flip it through the membrane to the exterior of the cell.

Once in the reducing conditions of the surrounding tissue, the dimer dissociates into

monomeric FGF1 that can enter systemic circulation or be sequestered in tissues

binding to heparan sulfate proteoglycans of the extracellular matrix. FGF1 can then

bind to and exert its effects via specific fibroblast growth factor receptor (FGFR)

proteins which themselves constitute a family of closely related molecules.

In addition to its extracellular activity, FGF1 can also function intracellularly. The

protein has a nuclear localization sequence (NLS) but the route that FGF1 takes to

get to the nucleus is unclear and it appears that some sort of cell surface receptor

binding is necessary, followed by its internalization and translocation to the nucleus

whereupon it can interact with nuclear isoforms of FGFRs. This is different from

FGF2 which also can activate nuclear FGFRs but has splicing variants of the protein

that never leave the cell and go directly to the nucleus.